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Glucose-6-phosphatase (G-6-Pase) (G6Pase) (EC 3.1.3.9) (Glucose-6-phosphatase alpha) (G6Pase-alpha)

 G6PC_HUMAN              Reviewed;         357 AA.
P35575; A1L4C0; B4E1C3; K7EL82;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 2.
13-FEB-2019, entry version 178.
RecName: Full=Glucose-6-phosphatase;
Short=G-6-Pase;
Short=G6Pase;
EC=3.1.3.9;
AltName: Full=Glucose-6-phosphatase alpha;
Short=G6Pase-alpha;
Name=G6PC; Synonyms=G6PT;
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 1).
TISSUE=Liver;
PubMed=8211187; DOI=10.1126/science.8211187;
Lei K.-J., Shelly L.L., Pan C.-J., Sidbury J.B., Chou J.Y.;
"Mutations in the glucose-6-phosphatase gene that cause glycogen
storage disease type 1a.";
Science 262:580-583(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
GLYCOSYLATION AT ASN-96.
PubMed=9705299; DOI=10.1074/jbc.273.34.21658;
Pan C.J., Lei K.J., Chou J.Y.;
"Asparagine-linked oligosaccharides are localized to a luminal
hydrophilic loop in human glucose-6-phosphatase.";
J. Biol. Chem. 273:21658-21662(1998).
[6]
ACTIVE SITES, MUTAGENESIS OF HIS-9; HIS-52; HIS-119; HIS-176; HIS-179;
HIS-197; HIS-252; HIS-307 AND HIS-353, AND CHARACTERIZATION OF
VARIANTS ASN-76; CYS-83 AND GLN-170.
PubMed=12093795; DOI=10.1074/jbc.M201853200;
Ghosh A., Shieh J.-J., Pan C.-J., Sun M.-S., Chou J.Y.;
"The catalytic center of glucose-6-phosphatase. HIS176 is the
nucleophile forming the phosphohistidine-enzyme intermediate during
catalysis.";
J. Biol. Chem. 277:32837-32842(2002).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[8]
VARIANT GSD1A CYS-83.
PubMed=8182131; DOI=10.1172/JCI117192;
Lei K.J., Pan C.J., Shelly L.L., Liu J.L., Chou J.Y.;
"Identification of mutations in the gene for glucose-6-phosphatase,
the enzyme deficient in glycogen storage disease type 1a.";
J. Clin. Invest. 93:1994-1999(1994).
[9]
VARIANTS GSD1A.
PubMed=7573034;
Lei K.-J., Chen Y.-T., Chen H., Wong L.-J.C., Liu J.-L.,
McConkie-Rosell A., van Hove J.L.K., Ou H.C.-Y., Yeh N.J., Pan L.Y.,
Chou J.Y.;
"Genetic basis of glycogen storage disease type 1a: prevalent
mutations at the glucose-6-phosphatase locus.";
Am. J. Hum. Genet. 57:766-771(1995).
[10]
VARIANTS GSD1A CYS-83 AND GLY-166.
PubMed=7623438; DOI=10.1007/BF00711368;
Parvari R., Moses S., Hershkovitz E., Carmi R., Bashan N.;
"Characterization of the mutations in the glucose-6-phosphatase gene
in Israeli patients with glycogen storage disease type 1a: R83C in six
Jews and a novel V166G mutation in a Muslim Arab.";
J. Inherit. Metab. Dis. 18:21-27(1995).
[11]
VARIANT GSD1A ILE-83.
PubMed=7655466; DOI=10.1093/hmg/4.6.1095;
Hwu W.-L., Chuang S.-C., Tsai L.-P., Chang M.-H., Chuang S.-M.,
Wang T.-R.;
"Glucose-6-phosphatase gene G327A mutation is common in Chinese
patients with glycogen storage disease type Ia.";
Hum. Mol. Genet. 4:1095-1096(1995).
[12]
VARIANTS GSD1A HIS-83 AND ASN-341.
PubMed=9001800;
Lee W.J., Lee H.M., Chi C.S., Shu S.G., Lin L.Y., Lin W.H.;
"Genetic analysis of the glucose-6-phosphatase mutation of type 1a
glycogen storage disease in a Chinese family.";
Clin. Genet. 50:206-211(1996).
[13]
VARIANTS GSD1A VAL-38; ARG-77; LYS-110; THR-124; GLU-184; ARG-188 AND
PRO-211.
PubMed=8733042; DOI=10.1136/jmg.33.5.358;
Chevalier-Porst F., Bozon D., Bonardot A.-M., Bruni N., Mithieux G.,
Mathieu M., Maire I.;
"Mutation analysis in 24 French patients with glycogen storage disease
type 1a.";
J. Med. Genet. 33:358-360(1996).
[14]
VARIANTS GSD1A CYS-83 AND GLY-166.
PubMed=9332655;
DOI=10.1002/(SICI)1096-8628(19971031)72:3<286::AID-AJMG6>3.0.CO;2-P;
Parvari R., Lei K.J., Bashan N., Hershkovitz E., Korman S.H.,
Barash V., Lerman-Sagie T., Mandel H., Chou J.Y., Moses S.W.;
"Glycogen storage disease type 1a in Israel: biochemical, clinical,
and mutational studies.";
Am. J. Med. Genet. 72:286-290(1997).
[15]
VARIANTS GSD1A CYS-83; GLN-170 AND TRP-270.
PubMed=9700612; DOI=10.1023/A:1005339616074;
Huener G., Podskarbi T., Schuetz M., Baykal T., Sarbat G., Shin Y.S.,
Demirkol M.;
"Molecular aspects of glycogen storage disease type Ia in Turkish
patients: a novel mutation in the glucose-6-phosphatase gene.";
J. Inherit. Metab. Dis. 21:445-446(1998).
[16]
VARIANT GSD1A ARG-68.
PubMed=9700613; DOI=10.1023/A:1005391600145;
Sartorato E.L., Reis F.C., Norato D.Y.J., Hackel C.;
"A novel mutation in a Brazilian patient with glycogen storage disease
type 1a.";
J. Inherit. Metab. Dis. 21:447-447(1998).
[17]
VARIANTS GSD1A CYS-83 AND LYS-264.
PubMed=9506659; DOI=10.1016/S0022-3476(98)70463-9;
Keller K.M., Schuetz M., Podskarbi T., Bindl L., Lentze M.J.,
Shin Y.S.;
"A new mutation of the glucose-6-phosphatase gene in a 4-year-old girl
with oligosymptomatic glycogen storage disease type 1a.";
J. Pediatr. 132:360-361(1998).
[18]
VARIANTS GSD1A VAL-266 AND PHE-338.
PubMed=10094563;
DOI=10.1002/(SICI)1098-1004(1999)13:2<173::AID-HUMU19>3.0.CO;2-E;
Rake J.P., ten Berge A.M., Verlind E., Visser G., Niezen-Koning K.E.,
Buys C.H.C.M., Smit G.P., Scheffer H.;
"Glycogen storage disease type Ia: four novel mutations (175delGG,
R170X, G266V and V338F) identified.";
Hum. Mutat. 13:173-173(1999).
[19]
VARIANTS GSD1A PRO-54 AND ILE-108.
PubMed=10447271;
DOI=10.1002/(SICI)1098-1004(1999)14:1<91::AID-HUMU21>3.0.CO;2-B;
Trioche P., Francoual J., Chalas J., Capel L., Bernard O., Labrune P.;
"Identification of three novel mutations (Q54P, W70X and T108I) in the
glucose-6-phosphatase gene of patients with glycogen storage disease
type Ia.";
Hum. Mutat. 14:91-91(1999).
[20]
VARIANTS GSD1A VAL-38; ARG-63; CYS-83; VAL-184; ARG-222; VAL-270;
CYS-295; PRO-298 AND PHE-338.
PubMed=10070617; DOI=10.1023/A:1005495131118;
Stroppiano M., Regis S., DiRocco M., Caroli F., Gandullia P.,
Gatti R.;
"Mutations in the glucose-6-phosphatase gene of 53 Italian patients
with glycogen storage disease type Ia.";
J. Inherit. Metab. Dis. 22:43-49(1999).
[21]
VARIANTS GSD1A HIS-83; ASP-122; PRO-179 AND LEU-257.
PubMed=10748407;
DOI=10.1002/(SICI)1096-8628(20000313)91:2<107::AID-AJMG5>3.0.CO;2-Y;
Akanuma J., Nishigaki T., Fujii K., Matsubara Y., Inui K.,
Takahashi K., Kure S., Suzuki Y., Ohura T., Miyabayashi S., Ogawa E.,
Iinuma K., Okada S., Narisawa K.;
"Glycogen storage disease type Ia: molecular diagnosis of 51 Japanese
patients and characterization of splicing mutations by analysis of
ectopically transcribed mRNA from lymphoblastoid cells.";
Am. J. Med. Genet. 91:107-112(2000).
[22]
VARIANTS GSD1A ARG-20; ARG-81; LEU-156 AND ASP-188.
PubMed=10612834;
DOI=10.1002/(SICI)1098-1004(200001)15:1<115::AID-HUMU23>3.0.CO;2-W;
Seydewitz H.H., Matern D.;
"Molecular genetic analysis of 40 patients with glycogen storage
disease type Ia: 100% mutation detection rate and 5 novel mutations.";
Hum. Mutat. 15:115-116(2000).
[23]
VARIANT GSD1A ALA-16.
PubMed=10738005;
DOI=10.1002/(SICI)1098-1004(200004)15:4<390::AID-HUMU32>3.0.CO;2-N;
Wu M.-C., Tsai F.-J., Lee C.-C., Lin S.-P., Wu J.-Y.;
"Identification of a novel missense mutation (T16A) in the glucose-6-
phosphatase gene in a Taiwan Chinese patient with glycogen storage
disease Ia (von Gierke disease).";
Hum. Mutat. 15:390-390(2000).
[24]
VARIANTS GSD1A ASN-76; ARG-77; CYS-83; ALA-166; ARG-188 AND CYS-295.
PubMed=10874313;
DOI=10.1002/1098-1004(200007)16:1<89::AID-HUMU17>3.3.CO;2-1;
Kozak L., Francova H., Hrabincova E., Stastna S., Peskova K.,
Elleder M.;
"Identification of mutations in the glucose-6-phosphatase gene in
Czech and Slovak patients with glycogen storage disease type Ia,
including novel mutations K76N, V166A and 540del5.";
Hum. Mutat. 16:89-89(2000).
[25]
VARIANTS GSD1A ARG-5; VAL-38; PRO-54; CYS-83; ILE-108; LYS-110;
ILE-111; GLU-184; ARG-188; THR-241; ARG-270; VAL-270; LEU-322; PHE-327
DEL AND PHE-338.
PubMed=11058903;
DOI=10.1002/1098-1004(200011)16:5<444::AID-HUMU10>3.0.CO;2-F;
Trioche P., Francoual J., Chalas J., Capel L., Lindenbaum A.,
Odievre M., Labrune P.;
"Genetic heterogeneity of glycogen storage disease type Ia in France:
a study of 48 patients.";
Hum. Mutat. 16:444-444(2000).
[26]
VARIANT GSD1A LEU-119.
PubMed=11058910;
DOI=10.1002/1098-1004(200011)16:5<447::AID-HUMU17>3.0.CO;2-M;
Wu M.-C., Tsai F.-J., Lee C.-C., Tsai C.-H., Wu J.-Y.;
"A novel missense mutation (H119L) identified in a Taiwan Chinese
family with glycogen storage disease Ia (von Gierke disease).";
Hum. Mutat. 16:447-447(2000).
[27]
VARIANT GSD1A ARG-188.
PubMed=10960498; DOI=10.1203/00006450-200009000-00011;
Weston B.W., Lin J.L., Muenzer J., Cameron H.S., Arnold R.R.,
Seydewitz H.H., Mayatepek E., Van Schaftingen E., Veiga-da-Cunha M.,
Matern D., Chen Y.T.;
"Glucose-6-phosphatase mutation G188R confers an atypical glycogen
storage disease type 1b phenotype.";
Pediatr. Res. 48:329-334(2000).
[28]
VARIANTS GSD1A ARG-20; VAL-38; PRO-65; ARG-68; ARG-77; ARG-81; CYS-83;
HIS-83; LYS-110; LEU-113; LEU-156; GLN-170; CYS-177; SER-178; ARG-188;
SER-188; ARG-236; PRO-265; VAL-270; PHE-327 DEL AND ARG-345.
PubMed=12373566; DOI=10.1007/BF02679989;
Matern D., Seydewitz H.H., Bali D., Lang C., Chen Y.-T.;
"Glycogen storage disease type I: diagnosis and phenotype/genotype
correlation.";
Eur. J. Pediatr. 161:S10-S19(2002).
[29]
VARIANT GSD1A CYS-83.
PubMed=15316959; DOI=10.1002/ajmg.a.30232;
Ekstein J., Rubin B.Y., Anderson S.L., Weinstein D.A., Bach G.,
Abeliovich D., Webb M., Risch N.;
"Mutation frequencies for glycogen storage disease Ia in the Ashkenazi
Jewish population.";
Am. J. Med. Genet. A 129:162-164(2004).
[30]
VARIANTS GSD1A ASP-122; ALA-178 AND ILE-255.
PubMed=15151508; DOI=10.1111/j.1399-0004.2004.00260.x;
Ki C.S., Han S.H., Kim H.J., Lee S.G., Kim E.J., Kim J.W., Choe Y.H.,
Seo J.K., Chang Y.J., Park J.Y.;
"Mutation spectrum of the glucose-6-phosphatase gene and its
implication in molecular diagnosis of Korean patients with glycogen
storage disease type Ia.";
Clin. Genet. 65:487-489(2004).
[31]
VARIANTS GSD1A ARG-16; PRO-54; CYS-83 AND CYS-209, AND
CHARACTERIZATION OF VARIANTS GSD1A ARG-16 AND CYS-209.
PubMed=15542400; DOI=10.1016/j.ymgme.2004.06.010;
Angaroni C.J., de Kremer R.D., Argarana C.E., Paschini-Capra A.E.,
Giner-Ayala A.N., Pezza R.J., Pan C.-J., Chou J.Y.;
"Glycogen storage disease type Ia in Argentina: two novel glucose-6-
phosphatase mutations affecting protein stability.";
Mol. Genet. Metab. 83:276-279(2004).
[32]
VARIANT [LARGE SCALE ANALYSIS] LEU-116.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the
endoplasmic reticulum. Forms with the glucose-6-phosphate
transporter (SLC37A4/G6PT) the complex responsible for glucose
production through glycogenolysis and gluconeogenesis. Hence, it
is the key enzyme in homeostatic regulation of blood glucose
levels.
-!- CATALYTIC ACTIVITY:
Reaction=D-glucose 6-phosphate + H2O = D-glucose + phosphate;
Xref=Rhea:RHEA:16689, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; EC=3.1.3.9;
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35575-1; Sequence=Displayed;
Name=2;
IsoId=P35575-2; Sequence=VSP_047558, VSP_047559;
Note=No experimental confirmation available.;
-!- DISEASE: Glycogen storage disease 1A (GSD1A) [MIM:232200]: A
metabolic disorder characterized by impairment of terminal steps
of glycogenolysis and gluconeogenesis. Patients manifest a wide
range of clinical symptoms and biochemical abnormalities,
including hypoglycemia, severe hepatomegaly due to excessive
accumulation of glycogen, kidney enlargement, growth retardation,
lactic acidemia, hyperlipidemia, and hyperuricemia.
{ECO:0000269|PubMed:10070617, ECO:0000269|PubMed:10094563,
ECO:0000269|PubMed:10447271, ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:10738005, ECO:0000269|PubMed:10748407,
ECO:0000269|PubMed:10874313, ECO:0000269|PubMed:10960498,
ECO:0000269|PubMed:11058903, ECO:0000269|PubMed:11058910,
ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:15151508,
ECO:0000269|PubMed:15316959, ECO:0000269|PubMed:15542400,
ECO:0000269|PubMed:7573034, ECO:0000269|PubMed:7623438,
ECO:0000269|PubMed:7655466, ECO:0000269|PubMed:8182131,
ECO:0000269|PubMed:8733042, ECO:0000269|PubMed:9001800,
ECO:0000269|PubMed:9332655, ECO:0000269|PubMed:9506659,
ECO:0000269|PubMed:9700612, ECO:0000269|PubMed:9700613}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG64735.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U01120; AAA16222.1; -; mRNA.
EMBL; AK303771; BAG64735.1; ALT_INIT; mRNA.
EMBL; AK313982; BAG36695.1; -; mRNA.
EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC130478; AAI30479.1; -; mRNA.
EMBL; BC136369; AAI36370.1; -; mRNA.
CCDS; CCDS11446.1; -. [P35575-1]
CCDS; CCDS59291.1; -. [P35575-2]
PIR; A48251; A48251.
RefSeq; NP_000142.2; NM_000151.3. [P35575-1]
RefSeq; NP_001257326.1; NM_001270397.1. [P35575-2]
UniGene; Hs.212293; -.
UniGene; Hs.742566; -.
ProteinModelPortal; P35575; -.
BioGrid; 108813; 3.
IntAct; P35575; 3.
STRING; 9606.ENSP00000253801; -.
BindingDB; P35575; -.
ChEMBL; CHEMBL2282; -.
DEPOD; P35575; -.
GlyConnect; 1267; -.
iPTMnet; P35575; -.
PhosphoSitePlus; P35575; -.
BioMuta; G6PC; -.
DMDM; 206729864; -.
PaxDb; P35575; -.
PeptideAtlas; P35575; -.
PRIDE; P35575; -.
ProteomicsDB; 55092; -.
DNASU; 2538; -.
Ensembl; ENST00000253801; ENSP00000253801; ENSG00000131482. [P35575-1]
Ensembl; ENST00000592383; ENSP00000465958; ENSG00000131482. [P35575-2]
GeneID; 2538; -.
KEGG; hsa:2538; -.
UCSC; uc002icb.3; human. [P35575-1]
CTD; 2538; -.
DisGeNET; 2538; -.
EuPathDB; HostDB:ENSG00000131482.9; -.
GeneCards; G6PC; -.
GeneReviews; G6PC; -.
HGNC; HGNC:4056; G6PC.
HPA; HPA052324; -.
MalaCards; G6PC; -.
MIM; 232200; phenotype.
MIM; 613742; gene.
neXtProt; NX_P35575; -.
OpenTargets; ENSG00000131482; -.
Orphanet; 79258; Glycogen storage disease due to glucose-6-phosphatase deficiency type Ia.
PharmGKB; PA28468; -.
eggNOG; ENOG410IDXG; Eukaryota.
eggNOG; ENOG4110AJ7; LUCA.
GeneTree; ENSGT00940000157844; -.
HOGENOM; HOG000264239; -.
HOVERGEN; HBG003560; -.
InParanoid; P35575; -.
KO; K01084; -.
OMA; RYLQVNY; -.
OrthoDB; 743717at2759; -.
PhylomeDB; P35575; -.
TreeFam; TF324388; -.
BioCyc; MetaCyc:HS05538-MONOMER; -.
BRENDA; 3.1.3.9; 2681.
Reactome; R-HSA-3274531; Glycogen storage disease type Ia (G6PC).
Reactome; R-HSA-70263; Gluconeogenesis.
Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
SABIO-RK; P35575; -.
SIGNOR; P35575; -.
UniPathway; UPA00138; -.
ChiTaRS; G6PC; human.
GeneWiki; G6PC; -.
GenomeRNAi; 2538; -.
PRO; PR:P35575; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131482; Expressed in 58 organ(s), highest expression level in liver.
ExpressionAtlas; P35575; baseline and differential.
Genevisible; P35575; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:UniProtKB.
GO; GO:0042301; F:phosphate ion binding; IMP:UniProtKB.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; IMP:UniProtKB.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0015760; P:glucose-6-phosphate transport; IEA:Ensembl.
GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0008202; P:steroid metabolic process; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0046415; P:urate metabolic process; IEA:Ensembl.
InterPro; IPR016275; Glucose-6-phosphatase.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
Pfam; PF01569; PAP2; 1.
PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Endoplasmic reticulum; Gluconeogenesis; Glycogen storage disease;
Glycoprotein; Hydrolase; Membrane; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 357 Glucose-6-phosphatase.
/FTId=PRO_0000087413.
TOPO_DOM 1 28 Lumenal. {ECO:0000255}.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TOPO_DOM 50 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TOPO_DOM 82 117 Lumenal. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TOPO_DOM 139 147 Cytoplasmic. {ECO:0000255}.
TRANSMEM 148 168 Helical. {ECO:0000255}.
TOPO_DOM 169 179 Lumenal. {ECO:0000255}.
TRANSMEM 180 202 Helical. {ECO:0000255}.
TOPO_DOM 203 209 Cytoplasmic. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 254 Lumenal. {ECO:0000255}.
TRANSMEM 255 275 Helical. {ECO:0000255}.
TOPO_DOM 276 291 Cytoplasmic. {ECO:0000255}.
TRANSMEM 292 312 Helical. {ECO:0000255}.
TOPO_DOM 313 320 Lumenal. {ECO:0000255}.
TRANSMEM 321 341 Helical. {ECO:0000255}.
TOPO_DOM 342 357 Cytoplasmic. {ECO:0000255}.
ACT_SITE 119 119 Proton donor. {ECO:0000255}.
ACT_SITE 176 176 Nucleophile.
{ECO:0000269|PubMed:12093795}.
BINDING 83 83 Substrate. {ECO:0000255}.
BINDING 170 170 Substrate. {ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9705299}.
VAR_SEQ 115 175 SPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVIL
WLGFWAVQLNVCLSRIYLAA -> KDKADLQISVLECHFVV
GILGCAAECLSVTNLPCCSFSSSSCCWSPVRHCCCRNFQPH
PQH (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047558.
VAR_SEQ 176 356 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047559.
VARIANT 5 5 M -> R (in GSD1A; dbSNP:rs1250172816).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046249.
VARIANT 16 16 T -> A (in GSD1A; dbSNP:rs761839506).
{ECO:0000269|PubMed:10738005}.
/FTId=VAR_046250.
VARIANT 16 16 T -> R (in GSD1A; complete loss of
activity and reduced enzyme stability).
{ECO:0000269|PubMed:15542400}.
/FTId=VAR_046251.
VARIANT 20 20 Q -> R (in GSD1A).
{ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_009202.
VARIANT 38 38 D -> V (in GSD1A; dbSNP:rs104894565).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005237.
VARIANT 54 54 Q -> P (in GSD1A; dbSNP:rs1057517008).
{ECO:0000269|PubMed:10447271,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:15542400}.
/FTId=VAR_009203.
VARIANT 63 63 W -> R (in GSD1A).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_046252.
VARIANT 65 65 A -> P (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046253.
VARIANT 68 68 G -> R (in GSD1A).
{ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:9700613}.
/FTId=VAR_046254.
VARIANT 76 76 K -> N (in GSD1A; loss of catalytic
activity). {ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:12093795}.
/FTId=VAR_046255.
VARIANT 77 77 W -> R (in GSD1A; dbSNP:rs104894566).
{ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005238.
VARIANT 81 81 G -> R (in GSD1A; dbSNP:rs756632286).
{ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_009204.
VARIANT 83 83 R -> C (in GSD1A; complete loss of
activity; prevalent mutation in Ashkenazi
Jewish population; dbSNP:rs1801175).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12093795,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:15316959,
ECO:0000269|PubMed:15542400,
ECO:0000269|PubMed:7623438,
ECO:0000269|PubMed:8182131,
ECO:0000269|PubMed:9332655,
ECO:0000269|PubMed:9506659,
ECO:0000269|PubMed:9700612}.
/FTId=VAR_005239.
VARIANT 83 83 R -> H (in GSD1A; dbSNP:rs1801176).
{ECO:0000269|PubMed:10748407,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:9001800}.
/FTId=VAR_005240.
VARIANT 83 83 R -> I (in GSD1A).
{ECO:0000269|PubMed:7655466}.
/FTId=VAR_005241.
VARIANT 108 108 T -> I (in GSD1A).
{ECO:0000269|PubMed:10447271,
ECO:0000269|PubMed:11058903}.
/FTId=VAR_009205.
VARIANT 110 110 E -> K (in GSD1A; dbSNP:rs104894567).
{ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005242.
VARIANT 111 111 T -> I (in GSD1A; dbSNP:rs1203167759).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046256.
VARIANT 113 113 P -> L (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046257.
VARIANT 116 116 P -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035922.
VARIANT 119 119 H -> L (in GSD1A; dbSNP:rs1401928680).
{ECO:0000269|PubMed:11058910}.
/FTId=VAR_046258.
VARIANT 122 122 G -> D (in GSD1A; dbSNP:rs759982943).
{ECO:0000269|PubMed:10748407,
ECO:0000269|PubMed:15151508}.
/FTId=VAR_046259.
VARIANT 124 124 A -> T (in GSD1A; dbSNP:rs104894568).
{ECO:0000269|PubMed:8733042}.
/FTId=VAR_005243.
VARIANT 156 156 W -> L (in GSD1A; dbSNP:rs1189630738).
{ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_009206.
VARIANT 166 166 V -> A (in GSD1A).
{ECO:0000269|PubMed:10874313}.
/FTId=VAR_046260.
VARIANT 166 166 V -> G (in GSD1A; complete loss of
activity; dbSNP:rs104894571).
{ECO:0000269|PubMed:7623438,
ECO:0000269|PubMed:9332655}.
/FTId=VAR_005244.
VARIANT 170 170 R -> Q (in GSD1A; loss of catalytic
activity; dbSNP:rs750470654).
{ECO:0000269|PubMed:12093795,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:9700612}.
/FTId=VAR_046261.
VARIANT 177 177 F -> C (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046262.
VARIANT 178 178 P -> A (in GSD1A; dbSNP:rs763543607).
{ECO:0000269|PubMed:15151508}.
/FTId=VAR_065164.
VARIANT 178 178 P -> S (in GSD1A; dbSNP:rs763543607).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046263.
VARIANT 179 179 H -> P (in GSD1A).
{ECO:0000269|PubMed:10748407}.
/FTId=VAR_046264.
VARIANT 184 184 G -> E (in GSD1A; dbSNP:rs104894569).
{ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005245.
VARIANT 184 184 G -> V (in GSD1A; dbSNP:rs104894569).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_046265.
VARIANT 188 188 G -> D (in GSD1A; dbSNP:rs760981149).
{ECO:0000269|PubMed:10612834}.
/FTId=VAR_009207.
VARIANT 188 188 G -> R (in GSD1A; complete loss of
activity; dbSNP:rs80356482).
{ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:10960498,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005246.
VARIANT 188 188 G -> S (in GSD1A; dbSNP:rs80356482).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046266.
VARIANT 209 209 Y -> C (in GSD1A; complete loss of
activity and reduced enzyme stability).
{ECO:0000269|PubMed:15542400}.
/FTId=VAR_046268.
VARIANT 211 211 L -> P (in GSD1A).
{ECO:0000269|PubMed:8733042}.
/FTId=VAR_005247.
VARIANT 222 222 G -> R (in GSD1A; dbSNP:rs1410392732).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_005248.
VARIANT 236 236 W -> R (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046269.
VARIANT 241 241 A -> T (in GSD1A).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046270.
VARIANT 255 255 T -> I (in GSD1A).
{ECO:0000269|PubMed:15151508}.
/FTId=VAR_065165.
VARIANT 257 257 P -> L (in GSD1A).
{ECO:0000269|PubMed:10748407}.
/FTId=VAR_046271.
VARIANT 264 264 N -> K (in GSD1A).
{ECO:0000269|PubMed:9506659}.
/FTId=VAR_046272.
VARIANT 265 265 L -> P (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046273.
VARIANT 266 266 G -> V (in GSD1A).
{ECO:0000269|PubMed:10094563}.
/FTId=VAR_005249.
VARIANT 270 270 G -> R (in GSD1A; dbSNP:rs1272803483).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046274.
VARIANT 270 270 G -> V (in GSD1A; dbSNP:rs80356483).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_005250.
VARIANT 270 270 G -> W (in GSD1A).
{ECO:0000269|PubMed:9700612}.
/FTId=VAR_046275.
VARIANT 295 295 R -> C (in GSD1A; dbSNP:rs104894563).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:10874313}.
/FTId=VAR_005251.
VARIANT 298 298 S -> P (in GSD1A; dbSNP:rs770003650).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_046276.
VARIANT 322 322 F -> L (in GSD1A; dbSNP:rs1399520060).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046277.
VARIANT 327 327 Missing (in GSD1A).
{ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_005252.
VARIANT 338 338 V -> F (in GSD1A; dbSNP:rs367727229).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:10094563,
ECO:0000269|PubMed:11058903}.
/FTId=VAR_005253.
VARIANT 341 341 I -> N (in GSD1A; dbSNP:rs387906505).
{ECO:0000269|PubMed:9001800}.
/FTId=VAR_005254.
VARIANT 345 345 L -> R (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046278.
MUTAGEN 9 9 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 52 52 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 119 119 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 176 176 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 179 179 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 197 197 H->T: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 252 252 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 307 307 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 353 353 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
CONFLICT 109 109 C -> R (in Ref. 2; BAG64735).
{ECO:0000305}.
CONFLICT 192 192 A -> T (in Ref. 1; AAA16222).
{ECO:0000305}.
SEQUENCE 357 AA; 40484 MW; 2FEA1C78928A9919 CRC64;
MEEGMNVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLQEAVGIK
LLWVAVIGDW LNLVFKWILF GQRPYWWVLD TDYYSNTSVP LIKQFPVTCE TGPGSPSGHA
MGTAGVYYVM VTSTLSIFQG KIKPTYRFRC LNVILWLGFW AVQLNVCLSR IYLAAHFPHQ
VVAGVLSGIA VAETFSHIHS IYNASLKKYF LITFFLFSFA IGFYLLLKGL GVDLLWTLEK
AQRWCEQPEW VHIDTTPFAS LLKNLGTLFG LGLALNSSMY RESCKGKLSK WLPFRLSSIV
ASLVLLHVFD SLKPPSQVEL VFYVLSFCKS AVVPLASVSV IPYCLAQVLG QPHKKSL


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Pathways :
WP1003: Ovarian Infertility Genes
WP1047: TNF-alpha NF-kB Signaling Pathway
WP109: UDP-Glucose Conversion
WP1120: Ovarian Infertility Genes
WP1163: TNF-alpha NF-kB Signaling Pathway
WP1209: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1340: Ovarian Infertility Genes
WP1369: TNF-alpha NF-kB Signaling Pathway
WP1434: Osteopontin Signaling
WP1487: TNF-alpha and mucus production in lung epythelium
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1571: EBV LMP1 signaling
WP1584: Type II diabetes mellitus
WP1614: 1- and 2-Methylnaphthalene degradation
WP1618: alpha-Linolenic acid metabolism
WP1652: Fructose and mannose metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1655: Geraniol degradation
WP1688: Polyketide sugar unit biosynthesis
WP1696: Riboflavin metabolism
WP1703: Streptomycin biosynthesis
WP1709: Thiamine metabolism

Related Genes :
[G6pc2 Igrp] Glucose-6-phosphatase 2 (G-6-Pase 2) (G6Pase 2) (EC 3.1.3.9) (Islet-specific glucose-6-phosphatase catalytic subunit-related protein)
[yihX b3885 JW5566] Alpha-D-glucose 1-phosphate phosphatase YihX (Alpha-D-glucose-1-P phosphatase) (EC 3.1.3.10) (Alpha-D-glucose-1-phosphatase) (Haloacid dehalogenase-like phosphatase 4) (HAD4)
[TPS1 BYP1 CIF1 FDP1 GGS1 GLC6 TSS1 YBR126C YBR0922] Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit (EC 2.4.1.15) (General glucose sensor subunit 1) (Glycogen metabolism control protein GLC6) (Trehalose synthase complex catalytic subunit TPS1) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase)
[cysQ Rv2131c MTCY270.37] 3'-phosphoadenosine 5'-phosphate phosphatase (PAP phosphatase) (EC 3.1.3.7) (3'(2'),5'-bisphosphate nucleotidase) (3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase) (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (DPNPase) (Fructose-1,6-bisphosphatase) (FBPase) (EC 3.1.3.11) (Inositol-1-monophosphatase) (I-1-Pase) (IMPase) (EC 3.1.3.25) (Inositol-1-phosphatase)
[RHM2 MUM4 At1g53500 F22G10.13 T3F20.18] Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2 (NDP-rhamnose synthase) (Protein MUCILAGE-MODIFIED 4) (Protein RHAMNOSE BIOSYNTHESIS 2) (Rhamnose biosynthetic enzyme 2) (AtRHM2) (UDP-L-rhamnose synthase MUM4) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)]
[RHM1 ROL1 At1g78570 T30F21.10] Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1 (Protein REPRESSOR OF LRX1 1) (Rhamnose biosynthetic enzyme 1) (AtRHM1) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)]
[hxpB yniC b1727 JW1716] Hexitol phosphatase B (2-deoxyglucose-6-phosphate phosphatase) (EC 3.1.3.68) (Mannitol-1-phosphatase) (EC 3.1.3.22) (Sorbitol-6-phosphatase) (EC 3.1.3.50) (Sugar-phosphatase) (EC 3.1.3.23)
[Ptpn6 Hcp Hcph Ptp1C] Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (70Z-SHP) (Hematopoietic cell protein-tyrosine phosphatase) (PTPTY-42) (Protein-tyrosine phosphatase 1C) (PTP-1C) (SH-PTP1) (SHP-1)
[Mtmr6] Myotubularin-related protein 6 (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)
[Gpi Gpi1] Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Autocrine motility factor) (AMF) (Neuroleukin) (NLK) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI)
[suhB MJ0109] Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (FBPase/IMPase) (EC 3.1.3.11) (EC 3.1.3.25) (Inositol-1-phosphatase) (I-1-Pase)
[fgd fgd1 MSMEG_0777 MSMEI_0761] F420-dependent glucose-6-phosphate dehydrogenase (FGD) (G6PD) (EC 1.1.98.2)
[Ppp2ca] Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16)
[Impad1 Impa3] Inositol monophosphatase 3 (IMP 3) (IMPase 3) (EC 3.1.3.25) (EC 3.1.3.7) (Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase) (Golgi-resident PAP phosphatase) (gPAPP) (Inositol monophosphatase domain-containing protein 1) (Inositol-1(or 4)-monophosphatase 3) (Myo-inositol monophosphatase A3)
[Ppp3ca Calna] Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (EC 3.1.3.16) (CAM-PRP catalytic subunit) (Calmodulin-dependent calcineurin A subunit alpha isoform) (CNA alpha)
[Pten Mmac1] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[RHM3 At3g14790 T21E2_4] Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3 (Probable rhamnose biosynthetic enzyme 3) (AtRHM3) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)]
[hxpA yfbT b2293 JW5376] Hexitol phosphatase A (Mannitol-1-phosphatase) (EC 3.1.3.22) (Sorbitol-6-phosphatase) (EC 3.1.3.50) (Sugar-phosphatase) (EC 3.1.3.23)
[fbp TK2164] Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13) (Fructose-1,6-bisphosphatase) (FBPase)
[Ptprn2] Receptor-type tyrosine-protein phosphatase N2 (R-PTP-N2) (EC 3.1.3.-) (EC 3.1.3.48) (PTP IA-2beta) (Phogrin) (Protein tyrosine phosphatase-NP) (PTP-NP) [Cleaved into: IA-2beta71; IA-2beta64; IA-2beta60]
[TPS2 PFK3 YDR074W YD8554.07] Trehalose-phosphatase (EC 3.1.3.12) (Trehalose synthase complex catalytic subunit TPS2) (Trehalose-6-phosphate phosphatase) (TPP)
[glvA glv-1 glvG malA BSU08180] Maltose-6'-phosphate glucosidase (EC 3.2.1.122) (6-phospho-alpha-D-glucosidase) (6-phosphoryl-O-alpha-D-glucopyranosyl:phosphoglucohydrolase)
[Rps6ka2 Mapkapk1c Rsk3] Ribosomal protein S6 kinase alpha-2 (S6K-alpha-2) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 2) (p90-RSK 2) (p90RSK2) (MAP kinase-activated protein kinase 1c) (MAPK-activated protein kinase 1c) (MAPKAP kinase 1c) (MAPKAPK-1c) (Protein-tyrosine kinase Mpk-9) (Ribosomal S6 kinase 3) (RSK-3) (pp90RSK3)
[Tigar] Fructose-2,6-bisphosphatase TIGAR (EC 3.1.3.46) (TP53-induced glycolysis and apoptosis regulator) (TP53-induced glycolysis regulatory phosphatase)
[Fto Kiaa1752] Alpha-ketoglutarate-dependent dioxygenase FTO (Fat mass and obesity-associated protein) (Protein fatso) (U6 small nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (EC 1.14.11.-) (U6 small nuclear RNA N(6)-methyladenosine-demethylase FTO) (EC 1.14.11.-) (mRNA (2'-O-methyladenosine-N(6)-)-demethylase FTO) (m6A(m)-demethylase FTO) (EC 1.14.11.-) (mRNA N(6)-methyladenosine demethylase FTO) (EC 1.14.11.53) (tRNA N1-methyl adenine demethylase FTO) (EC 1.14.11.-)
[Inppl1 Ship2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (AblSH3-binding protein) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[gpm2 Rv3214 LH57_17570] Acid phosphatase (EC 3.1.3.2) (Broad-specificity phosphatase) (Fructose-1,6-bisphosphatase) (FBPase) (EC 3.1.3.11)
[Nudt16] U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (m7GpppN-mRNA hydrolase)
[Ptpn11] Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) (Protein-tyrosine phosphatase SYP) (SH-PTP2) (SHP-2) (Shp2)

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