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GDP-L-galactose phosphorylase 1 (EC 2.7.7.69) (Protein VITAMIN C DEFECTIVE 2)

 GGAP1_ARATH             Reviewed;         442 AA.
Q8RWE8; Q8LKQ7; Q940B4; Q9SZ25;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
07-JUN-2017, entry version 84.
RecName: Full=GDP-L-galactose phosphorylase 1;
EC=2.7.7.69;
AltName: Full=Protein VITAMIN C DEFECTIVE 2;
Name=VTC2; OrderedLocusNames=At4g26850; ORFNames=F10M23.190;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-224 AND
SER-290.
PubMed=12068090; DOI=10.1104/pp.003533;
Jander G., Norris S.R., Rounsley S.D., Bush D.F., Levin I.M.,
Last R.L.;
"Arabidopsis map-based cloning in the post-genome era.";
Plant Physiol. 129:440-450(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
IDENTIFICATION.
PubMed=12119013; DOI=10.1021/bi025942q;
Brenner C.;
"Hint, Fhit, and GalT: function, structure, evolution, and mechanism
of three branches of the histidine triad superfamily of nucleotide
hydrolases and transferases.";
Biochemistry 41:9003-9014(2002).
[7]
INDUCTION BY JASMONATE AND OZONE.
PubMed=16262714; DOI=10.1111/j.1365-313X.2005.02560.x;
Sasaki-Sekimoto Y., Taki N., Obayashi T., Aono M., Matsumoto F.,
Sakurai N., Suzuki H., Hirai M.Y., Noji M., Saito K., Masuda T.,
Takamiya K., Shibata D., Ohta H.;
"Coordinated activation of metabolic pathways for antioxidants and
defence compounds by jasmonates and their roles in stress tolerance in
Arabidopsis.";
Plant J. 44:653-668(2005).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17462988; DOI=10.1074/jbc.M702094200;
Linster C.L., Gomez T.A., Christensen K.C., Adler L.N., Young B.D.,
Brenner C., Clarke S.G.;
"Arabidopsis VTC2 encodes a GDP-L-galactose phosphorylase, the last
unknown enzyme in the Smirnoff-Wheeler pathway to ascorbic acid in
plants.";
J. Biol. Chem. 282:18879-18885(2007).
[9]
FUNCTION, INDUCTION BY LIGHT, MUTAGENESIS OF GLY-224 AND SER-290,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
AND DISRUPTION PHENOTYPE.
PubMed=17877701; DOI=10.1111/j.1365-313X.2007.03266.x;
Dowdle J., Ishikawa T., Gatzek S., Rolinski S., Smirnoff N.;
"Two genes in Arabidopsis thaliana encoding GDP-L-galactose
phosphorylase are required for ascorbate biosynthesis and seedling
viability.";
Plant J. 52:673-689(2007).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17485667; DOI=10.1073/pnas.0701625104;
Laing W.A., Wright M.A., Cooney J., Bulley S.M.;
"The missing step of the L-galactose pathway of ascorbate biosynthesis
in plants, an L-galactose guanyltransferase, increases leaf ascorbate
content.";
Proc. Natl. Acad. Sci. U.S.A. 104:9534-9539(2007).
[11]
FUNCTION, AND MUTAGENESIS OF HIS-238.
PubMed=18463094; DOI=10.1074/jbc.M802594200;
Linster C.L., Adler L.N., Webb K., Christensen K.C., Brenner C.,
Clarke S.G.;
"A second GDP-L-galactose phosphorylase in arabidopsis en route to
vitamin C. Covalent intermediate and substrate requirements for the
conserved reaction.";
J. Biol. Chem. 283:18483-18492(2008).
[12]
INTERACTION WITH TLP1.
PubMed=17982713; DOI=10.1007/s10265-007-0118-8;
Ogura Y., Komatsu A., Zikihara K., Nanjo T., Tokutomi S., Wada M.,
Kiyosue T.;
"Blue light diminishes interaction of PAS/LOV proteins, putative blue
light receptors in Arabidopsis thaliana, with their interacting
partners.";
J. Plant Res. 121:97-105(2008).
[13]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
INDUCTION BY LIGHT.
PubMed=18516687; DOI=10.1007/s11103-008-9350-4;
Muller-Moule P.;
"An expression analysis of the ascorbate biosynthesis enzyme VTC2.";
Plant Mol. Biol. 68:31-41(2008).
-!- FUNCTION: Catalyzes a reaction of the Smirnoff-Wheeler pathway,
the major route to ascorbate biosynthesis in plants. Acts as a
phosphorylase rather than as a transferase. Uses preferentially
GDP-L-galactose and GDP-D-glucose as substrates. Lower activity
with GDP-L-fucose, very low activity with GDP-D-mannose, and no
activity with UDP-D-glucose, UDP-D-galactose or ADP-D-glucose.
Highly specific for inorganic phosphate as the guanylyl acceptor.
{ECO:0000269|PubMed:17462988, ECO:0000269|PubMed:17485667,
ECO:0000269|PubMed:17877701, ECO:0000269|PubMed:18463094}.
-!- CATALYTIC ACTIVITY: GDP-L-galactose + phosphate = alpha-L-
galactose 1-phosphate + GDP. {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17485667, ECO:0000269|PubMed:17877701}.
-!- ENZYME REGULATION: Not inhibited by dithiothreitol, N-
ethylmaleimide, phenylmethane sulfonyl fluoride, ascorbate, L-
galactose and L-galactonolactone.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.01 mM for GDP-L-galactose {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=0.0044 mM for GDP-D-glucose {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=0.52 mM for GDP-D-mannose {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=2.4 mM for phosphate {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=0.76 mM for phosphate {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=45 mM for L-galactose 1-phosphate
{ECO:0000269|PubMed:17462988, ECO:0000269|PubMed:17877701};
KM=29 mM for D-glucose 1-phosphate {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=54 mM for D-mannose 1-phosphate {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
KM=67 mM for D-galactose 1-phosphate
{ECO:0000269|PubMed:17462988, ECO:0000269|PubMed:17877701};
Note=The kinetic properties described in PubMed:17877701 differ
quite substantially from the ones shown here. This might be due
to the use of different enzyme activity assays.;
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:17462988,
ECO:0000269|PubMed:17877701};
-!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via GDP-
alpha-D-mannose pathway; L-ascorbate from GDP-alpha-D-mannose:
step 2/5.
-!- SUBUNIT: Interacts with TLP1. {ECO:0000269|PubMed:17982713}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18516687}.
Nucleus {ECO:0000269|PubMed:18516687}.
-!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flowers and
siliques. Highest expression in green tissues.
{ECO:0000269|PubMed:17877701, ECO:0000269|PubMed:18516687}.
-!- DEVELOPMENTAL STAGE: Expressed in all developmental stages.
{ECO:0000269|PubMed:18516687}.
-!- INDUCTION: By jasmonate, ozone and high light. Circadian-
regulation, with a peak in expression at the beginning of the
light cycle. {ECO:0000269|PubMed:16262714,
ECO:0000269|PubMed:17877701, ECO:0000269|PubMed:18516687}.
-!- DISRUPTION PHENOTYPE: Dwarf. 20% of the wild-type ascorbate level,
due to the partial redundancy with VTC5. Vtc2 and vtc5 double
mutants show growth arrest immediately upon germination and are
not viable. {ECO:0000269|PubMed:17877701}.
-!- SIMILARITY: Belongs to the GDPGP1 family. {ECO:0000305}.
-!- CAUTION: According to publications, it is related to the
galactose-1-phosphate uridylyltransferase type 1 family and
histidine triad superfamily (PubMed:12119013). However, such
families are not detected by prediction tools such as Pfam or
SUPFAM. {ECO:0000305|PubMed:12119013}.
-!- SEQUENCE CAUTION:
Sequence=AAM34266.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB36531.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB79540.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF508793; AAM34266.1; ALT_SEQ; Genomic_DNA.
EMBL; AL035440; CAB36531.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161565; CAB79540.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE85260.1; -; Genomic_DNA.
EMBL; AY056134; AAL07213.1; -; mRNA.
EMBL; AY093138; AAM13137.1; -; mRNA.
EMBL; BT006589; AAP31933.1; -; mRNA.
EMBL; AK226394; BAE98540.1; -; mRNA.
PIR; T04808; T04808.
RefSeq; NP_567759.1; NM_118819.3.
UniGene; At.23783; -.
UniGene; At.74980; -.
ProteinModelPortal; Q8RWE8; -.
BioGrid; 14079; 1.
IntAct; Q8RWE8; 1.
STRING; 3702.AT4G26850.1; -.
iPTMnet; Q8RWE8; -.
PaxDb; Q8RWE8; -.
EnsemblPlants; AT4G26850.1; AT4G26850.1; AT4G26850.
GeneID; 828792; -.
Gramene; AT4G26850.1; AT4G26850.1; AT4G26850.
KEGG; ath:AT4G26850; -.
Araport; AT4G26850; -.
TAIR; locus:2116342; AT4G26850.
eggNOG; KOG2720; Eukaryota.
eggNOG; ENOG4111FR6; LUCA.
HOGENOM; HOG000006065; -.
InParanoid; Q8RWE8; -.
KO; K14190; -.
OMA; NRTHGGP; -.
OrthoDB; EOG09360ACA; -.
PhylomeDB; Q8RWE8; -.
BioCyc; MetaCyc:AT4G26850-MONOMER; -.
BRENDA; 2.7.7.69; 399.
SABIO-RK; Q8RWE8; -.
UniPathway; UPA00990; UER00932.
PRO; PR:Q8RWE8; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; Q8RWE8; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0010475; F:galactose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; IDA:TAIR.
GO; GO:0010472; F:GDP-galactose:glucose-1-phosphate guanylyltransferase activity; IDA:TAIR.
GO; GO:0010471; F:GDP-galactose:mannose-1-phosphate guanylyltransferase activity; IDA:TAIR.
GO; GO:0010473; F:GDP-galactose:myoinositol-1-phosphate guanylyltransferase activity; IDA:TAIR.
GO; GO:0080047; F:GDP-L-galactose phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0010474; F:glucose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0008928; F:mannose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0080046; F:quercetin 4'-O-glucosyltransferase activity; IDA:TAIR.
GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
InterPro; IPR026506; GDPGP.
PANTHER; PTHR20884; PTHR20884; 1.
1: Evidence at protein level;
Ascorbate biosynthesis; Complete proteome; Cytoplasm;
Guanine-nucleotide releasing factor; Hydrolase; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
CHAIN 1 442 GDP-L-galactose phosphorylase 1.
/FTId=PRO_0000402541.
ACT_SITE 238 238 Tele-GMP-histidine intermediate.
{ECO:0000305}.
MUTAGEN 224 224 G->D: In vtc2-2; loss of activity; dwarf.
{ECO:0000269|PubMed:12068090,
ECO:0000269|PubMed:17877701}.
MUTAGEN 238 238 H->N: Strongly reduced activity.
{ECO:0000269|PubMed:18463094}.
MUTAGEN 290 290 S->F: In vtc2-3; strongly reduced
ascorbate levels.
{ECO:0000269|PubMed:12068090,
ECO:0000269|PubMed:17877701}.
CONFLICT 396 396 G -> S (in Ref. 4; AAL07213).
{ECO:0000305}.
SEQUENCE 442 AA; 48970 MW; 84C389ED098BBA2D CRC64;
MLKIKRVPTV VSNYQKDDGA EDPVGCGRNC LGACCLNGAR LPLYACKNLV KSGEKLVISH
EAIEPPVAFL ESLVLGEWED RFQRGLFRYD VTACETKVIP GKYGFVAQLN EGRHLKKRPT
EFRVDKVLQS FDGSKFNFTK VGQEELLFQF EAGEDAQVQF FPCMPIDPEN SPSVVAINVS
PIEYGHVLLI PRVLDCLPQR IDHKSLLLAV HMAAEAANPY FRLGYNSLGA FATINHLHFQ
AYYLAMPFPL EKAPTKKITT TVSGVKISEL LSYPVRSLLF EGGSSMQELS DTVSDCCVCL
QNNNIPFNIL ISDCGRQIFL MPQCYAEKQA LGEVSPEVLE TQVNPAVWEI SGHMVLKRKE
DYEGASEDNA WRLLAEASLS EERFKEVTAL AFEAIGCSNQ EEDLEGTIVH QQNSSGNVNQ
KSNRTHGGPI TNGTAAECLV LQ


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EIAAB10621 Bos taurus,Bovine,DCN1-like protein 3,DCUN1 domain-containing protein 3,DCUN1D3,Defective in cullin neddylation protein 1-like protein 3


 

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