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Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)

 G6PD_HUMAN              Reviewed;         515 AA.
P11413; D3DWX9; Q16000; Q16765; Q8IU70; Q8IU88; Q8IUA6; Q96PQ2;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 230.
RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
Short=G6PD;
EC=1.1.1.49;
Name=G6PD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=3515319; DOI=10.1093/nar/14.6.2511;
Persico M.G., Viglietto G., Martini G., Toniolo D., Paonessa G.,
Moscatelli C., Dono R., Vulliamy T.J., Luzzatto L., D'Urso M.;
"Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA
clones: primary structure of the protein and unusual 5' non-coding
region.";
Nucleic Acids Res. 14:2511-2522(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2428611;
Martini G., Toniolo D., Vulliamy T., Luzzatto L., Dono R.,
Viglietto G., Paonessa G., D'Urso M., Persico M.G.;
"Structural analysis of the X-linked gene encoding human glucose 6-
phosphate dehydrogenase.";
EMBO J. 5:1849-1855(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL NUCLEOTIDE
SEQUENCE [MRNA] (ISOFORM LONG), VARIANT NSHA MET-68, AND VARIANT
ASP-126.
PubMed=2836867; DOI=10.1073/pnas.85.11.3951;
Hirono A., Beutler E.;
"Molecular cloning and nucleotide sequence of cDNA for human glucose-
6-phosphate dehydrogenase variant A(-).";
Proc. Natl. Acad. Sci. U.S.A. 85:3951-3954(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NSHA MET-68, AND VARIANT
ASP-126.
PubMed=1889820; DOI=10.1016/0888-7543(91)90465-Q;
Chen E.Y., Cheng A., Lee A., Kuang W., Hillier L., Green P.,
Schlessinger D., Ciccodicola A., D'Urso M.;
"Sequence of human glucose-6-phosphate dehydrogenase cloned in
plasmids and a yeast artificial chromosome.";
Genomics 10:792-800(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NSHA MET-68, AND VARIANT
ASP-126.
PubMed=8733135; DOI=10.1093/hmg/5.5.659;
Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N.,
Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
D'Urso M.;
"Long-range sequence analysis in Xq28: thirteen known and six
candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
G6PD loci.";
Hum. Mol. Genet. 5:659-668(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-71.
PubMed=2758468; DOI=10.1016/0092-8674(89)90440-6;
Kanno H., Huang I.Y., Kan Y.W., Yoshida A.;
"Two structural genes on different chromosomes are required for
encoding the major subunit of human red cell glucose-6-phosphate
dehydrogenase.";
Cell 58:595-606(1989).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-71 (ISOFORM 3).
PubMed=8466644; DOI=10.1089/dna.1993.12.209;
Kanno H., Kondoh T., Yoshida A.;
"5' structure and expression of human glucose-6-phosphate
dehydrogenase mRNA.";
DNA Cell Biol. 12:209-215(1993).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=1874446; DOI=10.1016/0378-1119(91)90078-P;
Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.;
"The CpG island in the 5' region of the G6PD gene of man and mouse.";
Gene 102:197-203(1991).
[12]
PROTEIN SEQUENCE OF 2-9.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-34, AND VARIANT NSHA ARG-32.
PubMed=1945893; DOI=10.1093/nar/19.21.6056;
Chao L.T., Du C.S., Louie E., Zuo L., Chen E., Lubin B., Chiu D.T.;
"A to G substitution identified in exon 2 of the G6PD gene among G6PD
deficient Chinese.";
Nucleic Acids Res. 19:6056-6056(1991).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-515 (ISOFORM SHORT), VARIANT
NSHA MET-68, AND VARIANT ASP-126.
PubMed=12524354;
Saunders M.A., Hammer M.F., Nachman M.W.;
"Nucleotide variability at G6pd and the signature of malarial
selection in humans.";
Genetics 162:1849-1861(2002).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 154-515 (ISOFORM SHORT).
PubMed=3012556; DOI=10.1073/pnas.83.12.4157;
Takizawa T., Huang I.-Y., Ikuta T., Yoshida A.;
"Human glucose-6-phosphate dehydrogenase: primary structure and cDNA
cloning.";
Proc. Natl. Acad. Sci. U.S.A. 83:4157-4161(1986).
[16]
PROTEIN SEQUENCE OF 199-215.
PubMed=3126064; DOI=10.1111/j.1432-1033.1988.tb13815.x;
Camardella L., Caruso C., Rutigliano B., Romano M., di Prisco G.,
Descalzi-Cancedda F.;
"Human erythrocyte glucose-6-phosphate dehydrogenase. Identification
of a reactive lysyl residue labelled with pyridoxal 5'-phosphate.";
Eur. J. Biochem. 171:485-489(1988).
[17]
PROTEIN SEQUENCE OF 509-515.
PubMed=6696761; DOI=10.1016/0006-291X(84)91105-7;
Descalzi-Cancedda F., Caruso C., Romano M., di Prisco G.,
Camardella L.;
"Amino acid sequence of the carboxy-terminal end of human erythrocyte
glucose-6-phosphate dehydrogenase.";
Biochem. Biophys. Res. Commun. 118:332-338(1984).
[18]
ALTERNATIVE SPLICING.
PubMed=2910917; DOI=10.1172/JCI113881;
Hirono A., Beutler E.;
"Alternative splicing of human glucose-6-phosphate dehydrogenase
messenger RNA in different tissues.";
J. Clin. Invest. 83:343-346(1989).
[19]
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=7857286; DOI=10.1006/bbrc.1995.1192;
Camardella L., Damonte G., Carratore V., Benatti U., Tonetti M.,
Moneti G.;
"Glucose 6-phosphate dehydrogenase from human erythrocytes:
identification of N-acetyl-alanine at the N-terminus of the mature
protein.";
Biochem. Biophys. Res. Commun. 207:331-338(1995).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-171; LYS-403;
LYS-432 AND LYS-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
REVIEW.
PubMed=22431005; DOI=10.1002/iub.1017;
Stanton R.C.;
"Glucose-6-phosphate dehydrogenase, NADPH, and cell survival.";
IUBMB Life 64:362-369(2012).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-10 AND TYR-503,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
FUNCTION, ACETYLATION AT LYS-403 BY ELP3, DEACETYLATION AT LYS-403 BY
SIRT2, INTERACTION WITH SIRT2, MUTAGENESIS OF LYS-171; LYS-386 AND
LYS-403, AND SUBUNIT.
PubMed=24769394; DOI=10.1002/embj.201387224;
Wang Y.P., Zhou L.S., Zhao Y.Z., Wang S.W., Chen L.L., Liu L.X.,
Ling Z.Q., Hu F.J., Sun Y.P., Zhang J.Y., Yang C., Yang Y., Xiong Y.,
Guan K.L., Ye D.;
"Regulation of G6PD acetylation by KAT9/SIRT2 modulates NADPH
homeostasis and cell survival during oxidative stress.";
EMBO J. 33:1304-1320(2014).
[29]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF VARIANT CANTON IN COMPLEX
WITH NADP, AND SUBUNIT.
PubMed=10745013; DOI=10.1016/S0969-2126(00)00104-0;
Au S.W., Gover S., Lam V.M., Adams M.J.;
"Human glucose-6-phosphate dehydrogenase: the crystal structure
reveals a structural NADP(+) molecule and provides insights into
enzyme deficiency.";
Structure 8:293-303(2000).
[30]
REVIEW ON VARIANTS.
PubMed=8364584; DOI=10.1002/humu.1380020302;
Vulliamy T., Beutler E., Luzzatto L.;
"Variants of glucose-6-phosphate dehydrogenase are due to missense
mutations spread throughout the coding region of the gene.";
Hum. Mutat. 2:159-167(1993).
[31]
REVIEW ON VARIANTS.
PubMed=11857737; DOI=10.1002/humu.10036;
Kwok C.J., Martin A.C., Au S.W., Lam V.M.;
"G6PDdb, an integrated database of glucose-6-phosphate dehydrogenase
(G6PD) mutations.";
Hum. Mutat. 19:217-224(2002).
[32]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 28-514 IN COMPLEX WITH NADP
AND GLUCOSE 6-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=15858258; DOI=10.1107/S0907444905002350;
Kotaka M., Gover S., Vandeputte-Rutten L., Au S.W., Lam V.M.,
Adams M.J.;
"Structural studies of glucose-6-phosphate and NADP+ binding to human
glucose-6-phosphate dehydrogenase.";
Acta Crystallogr. D 61:495-504(2005).
[33]
VARIANT ASP-126.
PubMed=3446582; DOI=10.1016/0888-7543(87)90048-6;
Takizawa T., Yoneyama Y., Miwa S., Yoshida A.;
"A single nucleotide base transition is the basis of the common human
glucose-6-phosphate dehydrogenase variant A (+).";
Genomics 1:228-231(1987).
[34]
VARIANTS.
PubMed=3393536; DOI=10.1073/pnas.85.14.5171;
Vulliamy T.J., D'Urso M., Battistuzzi G., Estrada M., Foulkes N.S.,
Martini G., Calabro V., Poggi V., Giordano R., Town M., Luzzatto L.,
Persico M.G.;
"Diverse point mutations in the human glucose-6-phosphate
dehydrogenase gene cause enzyme deficiency and mild or severe
hemolytic anemia.";
Proc. Natl. Acad. Sci. U.S.A. 85:5171-5175(1988).
[35]
VARIANTS NSHA PHE-188 AND HIS-282.
PubMed=2912069;
de Vita G., Alcalay M., Sampietro M., Cappelini M.D., Fiorelli G.,
Toniolo D.;
"Two point mutations are responsible for G6PD polymorphism in
Sardinia.";
Am. J. Hum. Genet. 44:233-240(1989).
[36]
VARIANTS NSHA GLN-227; SER-353; CYS-387; LEU-394; ASP-410 AND PRO-439.
PubMed=1611091;
Beutler E., Westwood B., Prchal J.T., Vaca C.S., Bartsocas C.S.,
Baronciani L.;
"New glucose-6-phosphate dehydrogenase mutations from various ethnic
groups.";
Blood 80:255-256(1992).
[37]
VARIANT NSHA HIS-393.
PubMed=1536798; DOI=10.1111/j.1365-2141.1992.tb06409.x;
Filosa S., Calabro V., Vallone D., Poggi V., Mason P., Pagnini D.,
Alfinito F., Rotoli B., Martini G., Luzzatto L., Battistuzzi G.;
"Molecular basis of chronic non-spherocytic haemolytic anaemia: a new
G6PD variant (393arg-to-his) with abnormal K(m) G6P and marked in vivo
instability.";
Br. J. Haematol. 80:111-116(1992).
[38]
VARIANT NSHA CYS-454.
PubMed=1303180; DOI=10.1093/hmg/1.3.205;
Perng L.-I., Chiou S.-S., Liu T.-C., Chang J.-G.;
"A novel C to T substitution at nucleotide 1360 of cDNA which
abolishes a natural Hha I site accounts for a new G6PD deficiency gene
in Chinese.";
Hum. Mol. Genet. 1:205-205(1992).
[39]
VARIANT NSHA LYS-317.
PubMed=1303182; DOI=10.1093/hmg/1.3.209;
Ahluwalia A., Corcoran C.M., Vulliamy T.J., Ishwad C.S., Naidu J.M.,
Stevens D.J., Mason P.J., Luzzatto L.;
"G6PD Kalyan and G6PD Kerala; two deficient variants in India caused
by the same 317 Glu-->Lys mutation.";
Hum. Mol. Genet. 1:209-210(1992).
[40]
VARIANT NSHA THR-48.
PubMed=8490627; DOI=10.1093/hmg/2.1.81;
Nafa K., Reghis A., Osmani N., Baghli L., Benabadji M., Kaplan J.-C.,
Vulliamy T.J., Luzzatto L.;
"G6PD Aures: a new mutation (48 Ile-->Thr) causing mild G6PD
deficiency is associated with favism.";
Hum. Mol. Genet. 2:81-82(1993).
[41]
VARIANT NSHA GLY-176.
PubMed=8193373;
Hirono A., Miwa S., Fujii H., Ishida F., Yamada K., Kubota K.;
"Molecular study of eight Japanese cases of glucose-6-phosphate
dehydrogenase deficiency by nonradioisotopic single-strand
conformation polymorphism analysis.";
Blood 83:3363-3368(1994).
[42]
VARIANT NSHA LEU-396.
PubMed=7959695; DOI=10.1007/BF00211027;
Filosa S., Cai W., Galanello R., Cao A., de Mattia D., Schettini F.,
Martini G.;
"A novel single-base mutation in the glucose 6-phosphate dehydrogenase
gene is associated with chronic non-spherocytic haemolytic anaemia.";
Hum. Genet. 94:560-562(1994).
[43]
VARIANTS NAMORU; VANUA LAVA; NAONE AND UNION.
PubMed=7825590;
Ganczakowski M., Town M., Bowden D.K., Vulliamy T.J., Kaneko A.,
Clegg J.B., Weatherall D.J., Luzzatto L.;
"Multiple glucose 6-phosphate dehydrogenase-deficient variants
correlate with malaria endemicity in the Vanuatu archipelago
(southwestern Pacific).";
Am. J. Hum. Genet. 56:294-301(1995).
[44]
VARIANT NSHA GLY-44.
PubMed=8533762;
Kaeda J.S., Chhotray G.P., Ranjit M.R., Bautista J.M., Reddy P.H.,
Stevens D., Naidu J.M., Britt R.P., Vulliamy T.J., Luzzatto L.,
Mason P.J.;
"A new glucose-6-phosphate dehydrogenase variant, G6PD Orissa (44
Ala-->Gly), is the major polymorphic variant in tribal populations in
India.";
Am. J. Hum. Genet. 57:1335-1341(1995).
[45]
VARIANTS NSHA PRO-75; ASP-163; LYS-274 AND PHE-278.
PubMed=7858267;
Mason P.J., Sonati M.F., Macdonald D., Lanza C., Busutil D., Town M.,
Corcoran C.M., Kaeda J.S., Stevens D.J., Al-Ismail S., Altay C.,
Hatton C., Lewis D.S., McMullin M.F., Meloni T., Paul B., Pippard M.,
Prentice A.G., Vulliamy T.J., Luzzatto L.;
"New glucose-6-phosphate dehydrogenase mutations associated with
chronic anemia.";
Blood 85:1377-1380(1995).
[46]
VARIANT NSHA CYS-387, AND VARIANT ASP-126.
PubMed=9452072;
Vlachos A., Westwood B., Lipton J.M., Beutler E.;
"G6PD Mount Sinai: a new severe hemolytic variant characterized by
dual mutations at nucleotides 376G and 1159T (N126D).";
Hum. Mutat. Suppl. 1:S154-S155(1998).
[47]
VARIANT SINNAI LEU-12.
PubMed=10627140;
DOI=10.1002/(SICI)1098-1004(1998)12:1<72::AID-HUMU19>3.0.CO;2-T;
Galanello R., Loi D., Sollaino C., Dessi S., Cao A., Melis M.A.;
"A new glucose 6 phosphate dehydrogenase variant, G6PD Sinnai (34
G->T).";
Hum. Mutat. 12:72-73(1998).
[48]
VARIANT REHOVOT HIS-322.
PubMed=11112389; DOI=10.1006/bcmd.2000.0334;
Iancovici-Kidon M., Sthoeger D., Abrahamov A., Volach B., Beutler E.,
Gelbart T., Barak Y.;
"A new exon 9 glucose-6-phosphate dehydrogenase mutation (G6PD
'Rehovot') in a Jewish Ethiopian family with variable phenotypes.";
Blood Cells Mol. Dis. 26:567-571(2000).
[49]
ASSOCIATION OF VARIANT NSHA SER-163 WITH REDUCED DENSITY OF PLASMODIUM
VIVAX.
PubMed=20007901; DOI=10.1126/science.1178849;
Louicharoen C., Patin E., Paul R., Nuchprayoon I., Witoonpanich B.,
Peerapittayamongkol C., Casademont I., Sura T., Laird N.M.,
Singhasivanon P., Quintana-Murci L., Sakuntabhai A.;
"Positively selected G6PD-Mahidol mutation reduces Plasmodium vivax
density in Southeast Asians.";
Science 326:1546-1549(2009).
[50]
VARIANT NSHA SER-198, AND CHARACTERIZATION OF VARIANT NSHA SER-198.
PubMed=26479991; DOI=10.1097/MPH.0000000000000435;
Warny M., Lausen B., Birgens H., Knabe N., Petersen J.;
"Severe G6PD Deficiency Due to a New Missense Mutation in an Infant of
Northern European Descent.";
J. Pediatr. Hematol. Oncol. 37:E497-E499(2015).
[51]
VARIANT ASP-126.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Catalyzes the rate-limiting step of the oxidative
pentose-phosphate pathway, which represents a route for the
dissimilation of carbohydrates besides glycolysis. The main
function of this enzyme is to provide reducing power (NADPH) and
pentose phosphates for fatty acid and nucleic acid synthesis.
{ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394}.
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-
glucono-1,5-lactone + NADPH. {ECO:0000269|PubMed:15858258}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.07 uM for NADP {ECO:0000269|PubMed:15858258};
KM=52 uM for glucose 6-phosphate {ECO:0000269|PubMed:15858258};
-!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
step 1/3.
-!- SUBUNIT: Homotetramer; dimer of dimers. Interacts with SIRT2; the
interaction is enhanced by H(2)O(2) treatment.
{ECO:0000269|PubMed:10745013, ECO:0000269|PubMed:15858258,
ECO:0000269|PubMed:24769394}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-4289891, EBI-4289891;
P04792:HSPB1; NbExp=2; IntAct=EBI-4289891, EBI-352682;
Q8IXJ6:SIRT2; NbExp=3; IntAct=EBI-4289891, EBI-477232;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Short;
IsoId=P11413-1; Sequence=Displayed;
Name=Long;
IsoId=P11413-2; Sequence=VSP_001592;
Name=3;
IsoId=P11413-3; Sequence=VSP_037802;
Note=Contains a phosphoserine at position 26.
{ECO:0000244|PubMed:18669648};
-!- TISSUE SPECIFICITY: Isoform Long is found in lymphoblasts,
granulocytes and sperm.
-!- PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its
homodimerization and enzyme activity. Deacetylated by SIRT2 at
Lys-403; deacetylation stimulates its enzyme activity.
{ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:7857286}.
-!- POLYMORPHISM: The sequence shown is that of variant B, the most
common variant.
-!- DISEASE: Anemia, non-spherocytic hemolytic, due to G6PD deficiency
(NSHA) [MIM:300908]: A disease characterized by G6PD deficiency,
acute hemolytic anemia, fatigue, back pain, and jaundice. In most
patients, the disease is triggered by an exogenous agent, such as
some drugs, food, or infection. Increased unconjugated bilirubin,
lactate dehydrogenase, and reticulocytosis are markers of the
disorder. Although G6PD deficiency can be life-threatening, most
patients are asymptomatic throughout their life.
{ECO:0000269|PubMed:12524354, ECO:0000269|PubMed:1303180,
ECO:0000269|PubMed:1303182, ECO:0000269|PubMed:1536798,
ECO:0000269|PubMed:1611091, ECO:0000269|PubMed:1889820,
ECO:0000269|PubMed:1945893, ECO:0000269|PubMed:20007901,
ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:2836867,
ECO:0000269|PubMed:2912069, ECO:0000269|PubMed:7858267,
ECO:0000269|PubMed:7959695, ECO:0000269|PubMed:8193373,
ECO:0000269|PubMed:8490627, ECO:0000269|PubMed:8533762,
ECO:0000269|PubMed:8733135, ECO:0000269|PubMed:9452072}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. Deficiency of G6PD is associated with hemolytic anemia
in two different situations. First, in areas in which malaria has
been endemic, G6PD-deficiency alleles have reached high
frequencies (1% to 50%) and deficient individuals, though
essentially asymptomatic in the steady state, have a high risk of
acute hemolytic attacks. Secondly, sporadic cases of G6PD
deficiency occur at a very low frequencies, and they usually
present a more severe phenotype. Several types of NSHA are
recognized. Class-I variants are associated with severe NSHA;
class-II have an activity <10% of normal; class-III have an
activity of 10% to 60% of normal; class-IV have near normal
activity.
-!- MISCELLANEOUS: Binds two molecules of NADP. The first one is a
cosubstrate (bound to the N-terminal domain), the second is bound
to the C-terminal domain and functions as a structural element.
-!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA63175.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=G6PDdb; Note=G6PD mutation database;
URL="http://www.bioinf.org.uk/g6pd/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=G6PD";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X03674; CAA27309.1; -; mRNA.
EMBL; M65234; AAA63175.1; ALT_INIT; Genomic_DNA.
EMBL; M26749; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M26750; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65225; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65226; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65227; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65228; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65229; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65230; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65231; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65233; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M65232; AAA63175.1; JOINED; Genomic_DNA.
EMBL; M21248; AAA52500.1; -; mRNA.
EMBL; M19866; AAA52501.1; -; mRNA.
EMBL; X55448; CAA39089.1; -; Genomic_DNA.
EMBL; L44140; AAA92653.1; -; Genomic_DNA.
EMBL; AF277315; AAL27011.1; -; Genomic_DNA.
EMBL; CH471172; EAW72682.1; -; Genomic_DNA.
EMBL; CH471172; EAW72686.1; -; Genomic_DNA.
EMBL; BC000337; AAH00337.1; -; mRNA.
EMBL; M27940; AAA52504.1; -; mRNA.
EMBL; S58359; AAB26169.1; -; mRNA.
EMBL; X53815; CAA37811.1; -; Genomic_DNA.
EMBL; S64462; AAB20299.1; -; Genomic_DNA.
EMBL; AY158096; AAN76367.1; -; Genomic_DNA.
EMBL; AY158097; AAN76368.1; -; Genomic_DNA.
EMBL; AY158098; AAN76369.1; -; Genomic_DNA.
EMBL; AY158099; AAN76370.1; -; Genomic_DNA.
EMBL; AY158100; AAN76371.1; -; Genomic_DNA.
EMBL; AY158101; AAN76372.1; -; Genomic_DNA.
EMBL; AY158102; AAN76373.1; -; Genomic_DNA.
EMBL; AY158103; AAN76374.1; -; Genomic_DNA.
EMBL; AY158104; AAN76375.1; -; Genomic_DNA.
EMBL; AY158105; AAN76376.1; -; Genomic_DNA.
EMBL; AY158106; AAN76377.1; -; Genomic_DNA.
EMBL; AY158107; AAN76378.1; -; Genomic_DNA.
EMBL; AY158108; AAN76379.1; -; Genomic_DNA.
EMBL; AY158109; AAN76380.1; -; Genomic_DNA.
EMBL; AY158110; AAN76381.1; -; Genomic_DNA.
EMBL; AY158111; AAN76382.1; -; Genomic_DNA.
EMBL; AY158112; AAN76383.1; -; Genomic_DNA.
EMBL; AY158113; AAN76384.1; -; Genomic_DNA.
EMBL; AY158114; AAN76385.1; -; Genomic_DNA.
EMBL; AY158115; AAN76386.1; -; Genomic_DNA.
EMBL; AY158116; AAN76387.1; -; Genomic_DNA.
EMBL; AY158117; AAN76388.1; -; Genomic_DNA.
EMBL; AY158118; AAN76389.1; -; Genomic_DNA.
EMBL; AY158119; AAN76390.1; -; Genomic_DNA.
EMBL; AY158120; AAN76391.1; -; Genomic_DNA.
EMBL; AY158121; AAN76392.1; -; Genomic_DNA.
EMBL; AY158122; AAN76393.1; -; Genomic_DNA.
EMBL; AY158123; AAN76394.1; -; Genomic_DNA.
EMBL; AY158124; AAN76395.1; -; Genomic_DNA.
EMBL; AY158125; AAN76396.1; -; Genomic_DNA.
EMBL; AY158126; AAN76397.1; -; Genomic_DNA.
EMBL; AY158127; AAN76398.1; -; Genomic_DNA.
EMBL; AY158128; AAN76399.1; -; Genomic_DNA.
EMBL; AY158129; AAN76400.1; -; Genomic_DNA.
EMBL; AY158130; AAN76401.1; -; Genomic_DNA.
EMBL; AY158131; AAN76402.1; -; Genomic_DNA.
EMBL; AY158132; AAN76403.1; -; Genomic_DNA.
EMBL; AY158133; AAN76404.1; -; Genomic_DNA.
EMBL; AY158134; AAN76405.1; -; Genomic_DNA.
EMBL; AY158135; AAN76406.1; -; Genomic_DNA.
EMBL; AY158136; AAN76407.1; -; Genomic_DNA.
EMBL; AY158137; AAN76408.1; -; Genomic_DNA.
EMBL; AY158138; AAN76409.1; -; Genomic_DNA.
EMBL; AY158139; AAN76410.1; -; Genomic_DNA.
EMBL; AY158140; AAN76411.1; -; Genomic_DNA.
EMBL; AY158141; AAN76412.1; -; Genomic_DNA.
EMBL; AY158142; AAN76413.1; -; Genomic_DNA.
EMBL; M12996; AAA52499.1; -; mRNA.
EMBL; M23423; AAB59390.1; -; Genomic_DNA.
CCDS; CCDS14756.2; -. [P11413-3]
CCDS; CCDS44023.1; -. [P11413-1]
PIR; A40309; DEHUG6.
RefSeq; NP_000393.4; NM_000402.4. [P11413-3]
RefSeq; NP_001035810.1; NM_001042351.2. [P11413-1]
UniGene; Hs.461047; -.
UniGene; Hs.684904; -.
PDB; 1QKI; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-515.
PDB; 2BH9; X-ray; 2.50 A; A=27-515.
PDB; 2BHL; X-ray; 2.90 A; A/B=28-515.
PDB; 5UKW; X-ray; 2.65 A; A=29-511.
PDBsum; 1QKI; -.
PDBsum; 2BH9; -.
PDBsum; 2BHL; -.
PDBsum; 5UKW; -.
ProteinModelPortal; P11413; -.
SMR; P11413; -.
BioGrid; 108814; 67.
IntAct; P11413; 7.
MINT; MINT-4716941; -.
STRING; 9606.ENSP00000377192; -.
BindingDB; P11413; -.
ChEMBL; CHEMBL5347; -.
DrugBank; DB05107; 16-Bromoepiandrosterone.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB03085; Hydroxyacetic Acid.
iPTMnet; P11413; -.
PhosphoSitePlus; P11413; -.
SwissPalm; P11413; -.
DMDM; 116242483; -.
REPRODUCTION-2DPAGE; IPI00289800; -.
SWISS-2DPAGE; P11413; -.
EPD; P11413; -.
MaxQB; P11413; -.
PaxDb; P11413; -.
PeptideAtlas; P11413; -.
PRIDE; P11413; -.
DNASU; 2539; -.
Ensembl; ENST00000369620; ENSP00000358633; ENSG00000160211. [P11413-2]
Ensembl; ENST00000393562; ENSP00000377192; ENSG00000160211. [P11413-3]
Ensembl; ENST00000393564; ENSP00000377194; ENSG00000160211. [P11413-1]
Ensembl; ENST00000621232; ENSP00000483686; ENSG00000160211. [P11413-1]
GeneID; 2539; -.
KEGG; hsa:2539; -.
UCSC; uc004flx.3; human. [P11413-1]
CTD; 2539; -.
DisGeNET; 2539; -.
EuPathDB; HostDB:ENSG00000160211.15; -.
GeneCards; G6PD; -.
HGNC; HGNC:4057; G6PD.
HPA; HPA000247; -.
HPA; HPA000834; -.
MalaCards; G6PD; -.
MIM; 300908; phenotype.
MIM; 305900; gene.
neXtProt; NX_P11413; -.
OpenTargets; ENSG00000160211; -.
Orphanet; 362; Glucose-6-phosphate-dehydrogenase deficiency.
PharmGKB; PA28469; -.
eggNOG; KOG0563; Eukaryota.
eggNOG; COG0364; LUCA.
GeneTree; ENSGT00530000063435; -.
HOVERGEN; HBG000856; -.
InParanoid; P11413; -.
KO; K00036; -.
OMA; VEICVYE; -.
OrthoDB; EOG091G06FN; -.
PhylomeDB; P11413; -.
TreeFam; TF300584; -.
BioCyc; MetaCyc:HS08467-MONOMER; -.
BRENDA; 1.1.1.49; 2681.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-71336; Pentose phosphate pathway (hexose monophosphate shunt).
SABIO-RK; P11413; -.
SIGNOR; P11413; -.
UniPathway; UPA00115; UER00408.
ChiTaRS; G6PD; human.
EvolutionaryTrace; P11413; -.
GeneWiki; Glucose-6-phosphate_dehydrogenase; -.
GenomeRNAi; 2539; -.
PRO; PR:P11413; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000160211; -.
CleanEx; HS_G6PD; -.
ExpressionAtlas; P11413; baseline and differential.
Genevisible; P11413; HS.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005536; F:glucose binding; IDA:BHF-UCL.
GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050661; F:NADP binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:BHF-UCL.
GO; GO:0006695; P:cholesterol biosynthetic process; IMP:BHF-UCL.
GO; GO:0043249; P:erythrocyte maturation; IMP:BHF-UCL.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006749; P:glutathione metabolic process; IMP:BHF-UCL.
GO; GO:0006629; P:lipid metabolic process; TAS:BHF-UCL.
GO; GO:0006739; P:NADP metabolic process; IDA:UniProtKB.
GO; GO:0006740; P:NADPH regeneration; IMP:BHF-UCL.
GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
GO; GO:0010734; P:negative regulation of protein glutathionylation; IMP:BHF-UCL.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; IMP:BHF-UCL.
GO; GO:0019322; P:pentose biosynthetic process; IDA:BHF-UCL.
GO; GO:0006098; P:pentose-phosphate shunt; IDA:BHF-UCL.
GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:BHF-UCL.
GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IEA:Ensembl.
GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0010041; P:response to iron(III) ion; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0046390; P:ribose phosphate biosynthetic process; IMP:BHF-UCL.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
HAMAP; MF_00966; G6PD; 1.
InterPro; IPR001282; G6P_DH.
InterPro; IPR019796; G6P_DH_AS.
InterPro; IPR022675; G6P_DH_C.
InterPro; IPR022674; G6P_DH_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR23429; PTHR23429; 1.
Pfam; PF02781; G6PD_C; 1.
Pfam; PF00479; G6PD_N; 1.
PIRSF; PIRSF000110; G6PD; 1.
PRINTS; PR00079; G6PDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00871; zwf; 1.
PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
Disease mutation; Glucose metabolism; Hereditary hemolytic anemia;
NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:7857286}.
CHAIN 2 515 Glucose-6-phosphate 1-dehydrogenase.
/FTId=PRO_0000068083.
NP_BIND 38 45 NADP 1. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
NP_BIND 401 403 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
NP_BIND 421 423 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
REGION 201 205 Substrate binding.
ACT_SITE 263 263 Proton acceptor. {ECO:0000250}.
BINDING 72 72 NADP 1. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 147 147 NADP 1. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 171 171 NADP 1; via carbonyl oxygen.
{ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 171 171 Substrate.
BINDING 239 239 Substrate.
BINDING 258 258 Substrate.
BINDING 357 357 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 360 360 Substrate.
BINDING 365 365 Substrate.
BINDING 366 366 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 370 370 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 393 393 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 395 395 Substrate.
BINDING 487 487 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 503 503 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
BINDING 509 509 NADP 2. {ECO:0000269|PubMed:10745013,
ECO:0000269|PubMed:15858258}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:7857286}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 89 89 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 171 171 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 403 403 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:24769394}.
MOD_RES 432 432 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 497 497 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 503 503 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 1 M -> MGRRGSAPGNGRTLRGCERGGRRRRSADSVM (in
isoform 3). {ECO:0000303|PubMed:8466644}.
/FTId=VSP_037802.
VAR_SEQ 257 257 R -> RGPGRQGGSGSESCSLSLGSLVWGPHALEPGEQGGE
LRRALASSVPR (in isoform Long).
{ECO:0000305}.
/FTId=VSP_001592.
VARIANT 12 12 V -> L (in Sinnai).
{ECO:0000269|PubMed:10627140}.
/FTId=VAR_002450.
VARIANT 32 32 H -> R (in NSHA; Gahoe; class III;
frequent in Chinese; dbSNP:rs137852340).
{ECO:0000269|PubMed:1945893}.
/FTId=VAR_002451.
VARIANT 35 35 Missing (in NSHA; Sunderland; class I).
/FTId=VAR_002452.
VARIANT 44 44 A -> G (in NSHA; Orissa; class III;
frequent in Indian tribal populations;
dbSNP:rs78478128).
{ECO:0000269|PubMed:8533762}.
/FTId=VAR_002453.
VARIANT 48 48 I -> T (in NSHA; Aures; class II;
dbSNP:rs76645461).
{ECO:0000269|PubMed:8490627}.
/FTId=VAR_002454.
VARIANT 58 58 D -> N (in NSHA; Metaponto; class III;
dbSNP:rs137852315).
/FTId=VAR_002455.
VARIANT 68 68 V -> M (in NSHA; A(-) type I; class III;
frequent in African population;
dbSNP:rs1050828).
{ECO:0000269|PubMed:12524354,
ECO:0000269|PubMed:1889820,
ECO:0000269|PubMed:2836867,
ECO:0000269|PubMed:8733135}.
/FTId=VAR_002456.
VARIANT 70 70 Y -> H (in NSHA; Namoru; 4% activity;
dbSNP:rs137852349).
/FTId=VAR_002457.
VARIANT 75 75 L -> P (in NSHA; Swansea; class I).
{ECO:0000269|PubMed:7858267}.
/FTId=VAR_002458.
VARIANT 81 81 R -> C (in NSHA; Konan/Ube; class III;
dbSNP:rs138687036).
/FTId=VAR_002460.
VARIANT 81 81 R -> H (in NSHA; Lagosanto; class III;
dbSNP:rs782308266).
/FTId=VAR_002459.
VARIANT 106 106 S -> C (in NSHA; Vancouver; class I;
dbSNP:rs267606835).
/FTId=VAR_002461.
VARIANT 126 126 N -> D (polymorphism; found in Santa
Maria and Mount Sinai; associated with C-
387 in Mount Sinai; class IV and class I;
dbSNP:rs1050829).
{ECO:0000269|PubMed:12524354,
ECO:0000269|PubMed:1889820,
ECO:0000269|PubMed:27535533,
ECO:0000269|PubMed:2836867,
ECO:0000269|PubMed:3446582,
ECO:0000269|PubMed:8733135,
ECO:0000269|PubMed:9452072}.
/FTId=VAR_002462.
VARIANT 128 128 L -> P (in NSHA; Vanua Lava; 4% activity;
dbSNP:rs78365220).
/FTId=VAR_002463.
VARIANT 131 131 G -> V (in Chinese-4; dbSNP:rs137852341).
/FTId=VAR_002464.
VARIANT 156 156 E -> K (in NSHA; Ilesha; class III;
dbSNP:rs137852313).
/FTId=VAR_002465.
VARIANT 163 163 G -> D (in NSHA; Plymouth; class I).
{ECO:0000269|PubMed:7858267}.
/FTId=VAR_002467.
VARIANT 163 163 G -> S (in NSHA; Mahidol; class III;
associated with reduced density of
Plasmodium vivax but not Plasmodium
falciparum in Southeast Asians; reduced
activity; dbSNP:rs137852314).
/FTId=VAR_002466.
VARIANT 165 165 N -> D (in NSHA; Chinese-3; class II;
dbSNP:rs137852331).
/FTId=VAR_002468.
VARIANT 166 166 R -> H (in NSHA; Naone; 1% activity).
/FTId=VAR_002469.
VARIANT 176 176 D -> G (in NSHA; Shinshu; class I).
{ECO:0000269|PubMed:8193373}.
/FTId=VAR_002470.
VARIANT 181 181 D -> V (in NSHA; Santa Maria; class I;
dbSNP:rs5030872).
/FTId=VAR_002471.
VARIANT 182 182 R -> W (in NSHA; Vancouver; class I;
dbSNP:rs267606836).
/FTId=VAR_002472.
VARIANT 188 188 S -> F (in NSHA; Sassari/Cagliari; class
II; frequent in the Mediterranean;
dbSNP:rs5030868).
{ECO:0000269|PubMed:2912069}.
/FTId=VAR_002473.
VARIANT 198 198 R -> C (in NSHA; Coimbra; class II;
dbSNP:rs137852330).
/FTId=VAR_002474.
VARIANT 198 198 R -> P (in NSHA; Santiago; class I;
dbSNP:rs137852332).
/FTId=VAR_002475.
VARIANT 198 198 R -> S (in NSHA; Herlev; no
glucoshosphate dehydrogenase activity).
{ECO:0000269|PubMed:26479991}.
/FTId=VAR_075555.
VARIANT 212 212 M -> V (in NSHA; Sibari; class III;
dbSNP:rs782754619).
/FTId=VAR_002476.
VARIANT 213 213 V -> L (in NSHA; Minnesota; class I;
dbSNP:rs137852326).
/FTId=VAR_002477.
VARIANT 216 216 F -> L (in NSHA; Harilaou; class I;
dbSNP:rs137852319).
/FTId=VAR_002478.
VARIANT 227 227 R -> L (in NSHA; A- type 2; class III;
dbSNP:rs137852328).
/FTId=VAR_002480.
VARIANT 227 227 R -> Q (in NSHA; Mexico City; class III;
dbSNP:rs137852328).
{ECO:0000269|PubMed:1611091}.
/FTId=VAR_002479.
VARIANT 242 243 Missing (in NSHA; Stonybrook; class I).
/FTId=VAR_002481.
VARIANT 257 257 R -> G (in NSHA; Wayne; class I).
/FTId=VAR_002482.
VARIANT 274 274 E -> K (in NSHA; Corum; class I).
{ECO:0000269|PubMed:7858267}.
/FTId=VAR_002483.
VARIANT 278 278 S -> F (in NSHA; Wexham; class I).
{ECO:0000269|PubMed:7858267}.
/FTId=VAR_002484.
VARIANT 279 279 T -> S (in NSHA; Chinese-1; class II).
/FTId=VAR_002485.
VARIANT 282 282 D -> H (in NSHA; Seattle; class III;
dbSNP:rs137852318).
{ECO:0000269|PubMed:2912069}.
/FTId=VAR_002486.
VARIANT 285 285 R -> H (in NSHA; Montalbano; class III;
dbSNP:rs74575103).
/FTId=VAR_002487.
VARIANT 291 291 V -> M (in NSHA; Viangchan/Jammu; class
II; dbSNP:rs137852327).
/FTId=VAR_002488.
VARIANT 317 317 E -> K (in NSHA; Kalyan/Kerala; class
III; dbSNP:rs137852339).
{ECO:0000269|PubMed:1303182}.
/FTId=VAR_002489.
VARIANT 322 322 Y -> H (in Rehovot; dbSNP:rs137852347).
{ECO:0000269|PubMed:11112389}.
/FTId=VAR_020535.
VARIANT 323 323 L -> P (in NSHA; A- type 3; class III;
dbSNP:rs76723693).
/FTId=VAR_002490.
VARIANT 335 335 A -> T (in NSHA; Chatham; class III;
dbSNP:rs5030869).
/FTId=VAR_002491.
VARIANT 342 342 L -> F (in Chinese-5; dbSNP:rs137852342).
/FTId=VAR_002492.
VARIANT 353 353 P -> S (in NSHA; Ierapetra; class II;
dbSNP:rs137852333).
{ECO:0000269|PubMed:1611091}.
/FTId=VAR_002493.
VARIANT 363 363 N -> K (in NSHA; Loma Linda; class I;
dbSNP:rs137852329).
/FTId=VAR_002494.
VARIANT 385 385 C -> R (in NSHA; Tomah; class I;
dbSNP:rs137852322).
/FTId=VAR_002495.
VARIANT 386 386 K -> E (in NSHA; Iowa; class I;
dbSNP:rs137852320).
/FTId=VAR_002496.
VARIANT 387 387 R -> C (in NSHA; Guadajalara and Mount
Sinai; class I; dbSNP:rs137852334).
{ECO:0000269|PubMed:1611091,
ECO:0000269|PubMed:9452072}.
/FTId=VAR_002498.
VARIANT 387 387 R -> H (in NSHA; Beverly Hills; class I;
dbSNP:rs137852321).
/FTId=VAR_002497.
VARIANT 393 393 R -> H (in NSHA; Nashville/Anaheim; class
I; dbSNP:rs137852316).
{ECO:0000269|PubMed:1536798}.
/FTId=VAR_002499.
VARIANT 394 394 V -> L (in NSHA; Alhambra; class I;
dbSNP:rs137852335).
{ECO:0000269|PubMed:1611091}.
/FTId=VAR_002500.
VARIANT 396 396 P -> L (in NSHA; Bari; class I).
{ECO:0000269|PubMed:7959695}.
/FTId=VAR_002501.
VARIANT 398 398 E -> K (in NSHA; Puerto Limon; class I;
dbSNP:rs137852325).
/FTId=VAR_002502.
VARIANT 410 410 G -> C (in NSHA; Riverside; class I;
dbSNP:rs137852323).
/FTId=VAR_002503.
VARIANT 410 410 G -> D (in NSHA; Japan; class I;
dbSNP:rs137852336).
{ECO:0000269|PubMed:1611091}.
/FTId=VAR_002504.
VARIANT 416 416 E -> K (in NSHA; Tokyo; class I).
/FTId=VAR_002505.
VARIANT 439 439 R -> P (in NSHA; Pawnee; class I;
dbSNP:rs137852337).
{ECO:0000269|PubMed:1611091}.
/FTId=VAR_002506.
VARIANT 440 440 L -> F (in NSHA; Telti/Kobe; class I).
/FTId=VAR_002507.
VARIANT 447 447 G -> R (in NSHA; Santiago de Cuba; class
I; dbSNP:rs137852317).
/FTId=VAR_002508.
VARIANT 449 449 Q -> H (in NSHA; Cassano; class II).
/FTId=VAR_002509.
VARIANT 454 454 R -> C (in NSHA; Chinese-II/Maewo/Union;
class II; <1% activity;
dbSNP:rs398123546).
{ECO:0000269|PubMed:1303180}.
/FTId=VAR_002510.
VARIANT 454 454 R -> H (in NSHA; Andalus; class I;
dbSNP:rs137852324).
/FTId=VAR_002511.
VARIANT 459 459 R -> L (in NSHA; Canton; class II;
frequent in China; dbSNP:rs72554665).
/FTId=VAR_002512.
VARIANT 459 459 R -> P (in NSHA; Cosenza; class II;
dbSNP:rs72554665).
/FTId=VAR_002513.
VARIANT 463 463 R -> H (in NSHA; Kaiping; class II;
dbSNP:rs72554664).
/FTId=VAR_002514.
VARIANT 488 488 G -> V (in NSHA; Campinas; class I).
/FTId=VAR_002515.
MUTAGEN 171 171 K->Q: Inhibits catalytic activity. Does
not impair dimerization.
{ECO:0000269|PubMed:24769394}.
MUTAGEN 171 171 K->R: Inhibits catalytic activity. Does
not impair dimerization.
{ECO:0000269|PubMed:24769394}.
MUTAGEN 386 386 K->Q: Impairs dimerization and reduces
catalytic activity.
{ECO:0000269|PubMed:24769394}.
MUTAGEN 386 386 K->R: Does not impair dimerization and
catalytic activity.
{ECO:0000269|PubMed:24769394}.
MUTAGEN 403 403 K->Q: Impairs dimerization and reduces
catalytic activity in cells under
oxidative stress.
{ECO:0000269|PubMed:24769394}.
MUTAGEN 403 403 K->R: Does not impair dimerization and
catalytic activity.
{ECO:0000269|PubMed:24769394}.
CONFLICT 11 11 Q -> H (in Ref. 1; CAA27309, 2; AAA63175
and 3; AAA52500). {ECO:0000305}.
CONFLICT 435 436 DA -> EP (in Ref. 15; AAA52499).
{ECO:0000305}.
STRAND 32 37 {ECO:0000244|PDB:2BH9}.
TURN 38 40 {ECO:0000244|PDB:2BH9}.
HELIX 42 46 {ECO:0000244|PDB:2BH9}.
HELIX 48 57 {ECO:0000244|PDB:2BH9}.
STRAND 63 73 {ECO:0000244|PDB:2BH9}.
HELIX 77 84 {ECO:0000244|PDB:2BH9}.
HELIX 85 87 {ECO:0000244|PDB:2BH9}.
HELIX 92 94 {ECO:0000244|PDB:2BH9}.
HELIX 95 103 {ECO:0000244|PDB:2BH9}.
STRAND 105 109 {ECO:0000244|PDB:2BH9}.
HELIX 115 126 {ECO:0000244|PDB:2BH9}.
TURN 127 133 {ECO:0000244|PDB:2BH9}.
STRAND 134 140 {ECO:0000244|PDB:2BH9}.
TURN 144 146 {ECO:0000244|PDB:2BHL}.
HELIX 147 157 {ECO:0000244|PDB:2BH9}.
STRAND 161 163 {ECO:0000244|PDB:2BH9}.
STRAND 165 169 {ECO:0000244|PDB:2BH9}.
HELIX 177 187 {ECO:0000244|PDB:2BH9}.
TURN 188 190 {ECO:0000244|PDB:2BH9}.
HELIX 193 195 {ECO:0000244|PDB:2BH9}.
STRAND 196 198 {ECO:0000244|PDB:2BH9}.
HELIX 201 204 {ECO:0000244|PDB:2BH9}.
HELIX 206 216 {ECO:0000244|PDB:2BH9}.
HELIX 219 221 {ECO:0000244|PDB:2BH9}.
STRAND 222 226 {ECO:0000244|PDB:2BHL}.
TURN 227 229 {ECO:0000244|PDB:2BH9}.
STRAND 230 238 {ECO:0000244|PDB:2BH9}.
HELIX 247 250 {ECO:0000244|PDB:2BH9}.
TURN 251 253 {ECO:0000244|PDB:2BH9}.
HELIX 254 258 {ECO:0000244|PDB:2BH9}.
TURN 259 262 {ECO:0000244|PDB:2BH9}.
HELIX 263 272 {ECO:0000244|PDB:2BH9}.
STRAND 277 280 {ECO:0000244|PDB:2BH9}.
HELIX 281 292 {ECO:0000244|PDB:2BH9}.
HELIX 300 302 {ECO:0000244|PDB:2BH9}.
STRAND 303 309 {ECO:0000244|PDB:2BH9}.
HELIX 317 319 {ECO:0000244|PDB:2BHL}.
HELIX 322 324 {ECO:0000244|PDB:2BH9}.
STRAND 326 328 {ECO:0000244|PDB:2BHL}.
STRAND 336 344 {ECO:0000244|PDB:2BH9}.
TURN 347 351 {ECO:0000244|PDB:2BH9}.
STRAND 353 361 {ECO:0000244|PDB:2BH9}.
STRAND 366 373 {ECO:0000244|PDB:2BH9}.
STRAND 389 397 {ECO:0000244|PDB:2BH9}.
STRAND 399 407 {ECO:0000244|PDB:2BH9}.
TURN 409 411 {ECO:0000244|PDB:2BH9}.
STRAND 414 423 {ECO:0000244|PDB:2BH9}.
TURN 424 426 {ECO:0000244|PDB:2BH9}.
STRAND 427 431 {ECO:0000244|PDB:2BH9}.
HELIX 436 446 {ECO:0000244|PDB:2BH9}.
HELIX 449 451 {ECO:0000244|PDB:1QKI}.
HELIX 455 475 {ECO:0000244|PDB:2BH9}.
STRAND 480 483 {ECO:0000244|PDB:2BH9}.
STRAND 486 488 {ECO:0000244|PDB:2BH9}.
HELIX 490 498 {ECO:0000244|PDB:2BH9}.
SEQUENCE 515 AA; 59257 MW; F2B775340640A96F CRC64;
MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL
LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED FFARNSYVAG QYDDAASYQR
LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS QIGWNRIIVE KPFGRDLQSS
DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP
FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA
NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK
ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL
DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH QIELEKPKPI
PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL


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