GGAP2_ARATH
ID GGAP2_ARATH Reviewed; 431 AA.
AC Q9FLP9;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=GDP-L-galactose phosphorylase 2;
DE EC=2.7.7.69;
DE AltName: Full=Protein VITAMIN C DEFECTIVE 5;
GN Name=VTC5; Synonyms=VTC2L; OrderedLocusNames=At5g55120; ORFNames=MCO15.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION BY JASMONATE AND OZONE.
RX PubMed=16262714; DOI=10.1111/j.1365-313x.2005.02560.x;
RA Sasaki-Sekimoto Y., Taki N., Obayashi T., Aono M., Matsumoto F.,
RA Sakurai N., Suzuki H., Hirai M.Y., Noji M., Saito K., Masuda T.,
RA Takamiya K., Shibata D., Ohta H.;
RT "Coordinated activation of metabolic pathways for antioxidants and defence
RT compounds by jasmonates and their roles in stress tolerance in
RT Arabidopsis.";
RL Plant J. 44:653-668(2005).
RN [5]
RP FUNCTION, INDUCTION BY LIGHT, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17877701; DOI=10.1111/j.1365-313x.2007.03266.x;
RA Dowdle J., Ishikawa T., Gatzek S., Rolinski S., Smirnoff N.;
RT "Two genes in Arabidopsis thaliana encoding GDP-L-galactose phosphorylase
RT are required for ascorbate biosynthesis and seedling viability.";
RL Plant J. 52:673-689(2007).
RN [6]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=17485667; DOI=10.1073/pnas.0701625104;
RA Laing W.A., Wright M.A., Cooney J., Bulley S.M.;
RT "The missing step of the L-galactose pathway of ascorbate biosynthesis in
RT plants, an L-galactose guanyltransferase, increases leaf ascorbate
RT content.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9534-9539(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18463094; DOI=10.1074/jbc.m802594200;
RA Linster C.L., Adler L.N., Webb K., Christensen K.C., Brenner C.,
RA Clarke S.G.;
RT "A second GDP-L-galactose phosphorylase in arabidopsis en route to vitamin
RT C. Covalent intermediate and substrate requirements for the conserved
RT reaction.";
RL J. Biol. Chem. 283:18483-18492(2008).
RN [8]
RP INTERACTION WITH TLP1.
RX PubMed=17982713; DOI=10.1007/s10265-007-0118-8;
RA Ogura Y., Komatsu A., Zikihara K., Nanjo T., Tokutomi S., Wada M.,
RA Kiyosue T.;
RT "Blue light diminishes interaction of PAS/LOV proteins, putative blue light
RT receptors in Arabidopsis thaliana, with their interacting partners.";
RL J. Plant Res. 121:97-105(2008).
CC -!- FUNCTION: Catalyzes a reaction of the Smirnoff-Wheeler pathway, the
CC major route to ascorbate biosynthesis in plants. Acts as a
CC phosphorylase rather than as a transferase. Uses preferentially GDP-L-
CC galactose and GDP-D-glucose as substrates. Lower activity with GDP-L-
CC fucose, very low activity with GDP-D-mannose, and no activity with UDP-
CC D-glucose, UDP-D-galactose or ADP-D-glucose. Highly specific for
CC inorganic phosphate as the guanylyl acceptor.
CC {ECO:0000269|PubMed:17485667, ECO:0000269|PubMed:17877701,
CC ECO:0000269|PubMed:18463094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-galactose + phosphate = beta-L-galactose 1-
CC phosphate + GDP + H(+); Xref=Rhea:RHEA:27698, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:61454,
CC ChEBI:CHEBI:75522; EC=2.7.7.69;
CC Evidence={ECO:0000269|PubMed:18463094};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0083 mM for GDP-L-galactose {ECO:0000269|PubMed:18463094};
CC KM=0.667 mM for GDP-L-galactose {ECO:0000269|PubMed:17877701};
CC KM=0.012 mM for GDP-D-glucose {ECO:0000269|PubMed:18463094};
CC KM=1.3 mM for GDP-D-mannose {ECO:0000269|PubMed:18463094};
CC KM=1.0 mM for phosphate (in the presence of GDP-L-galactose)
CC {ECO:0000269|PubMed:18463094};
CC KM=0.22 mM for phosphate (in the presence of GDP-D-glucose)
CC {ECO:0000269|PubMed:18463094};
CC KM=0.13 mM for phosphate {ECO:0000269|PubMed:17877701};
CC KM=16 mM for L-galactose 1-phosphate {ECO:0000269|PubMed:18463094};
CC KM=10 mM for D-glucose 1-phosphate {ECO:0000269|PubMed:18463094};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via GDP-alpha-
CC D-mannose pathway; L-ascorbate from GDP-alpha-D-mannose: step 2/5.
CC -!- SUBUNIT: Interacts with TLP1. {ECO:0000269|PubMed:17982713}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flowers and
CC siliques. {ECO:0000269|PubMed:17877701}.
CC -!- INDUCTION: By jasmonate, ozone and high light. Circadian-regulation,
CC with a peak in expression at the beginning of the light cycle.
CC {ECO:0000269|PubMed:16262714, ECO:0000269|PubMed:17877701}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and slightly decreased
CC ascorbate levels; due to the partial redundancy with VTC2. Vtc2 and
CC vtc5 double mutants show growth arrest immediately upon germination and
CC are not viable. {ECO:0000269|PubMed:17877701}.
CC -!- SIMILARITY: Belongs to the GDPGP1 family. {ECO:0000305}.
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DR EMBL; AB010071; BAB08581.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96583.1; -; Genomic_DNA.
DR EMBL; AY063788; AAL36095.1; -; mRNA.
DR EMBL; AY091285; AAM14224.1; -; mRNA.
DR RefSeq; NP_200323.1; NM_124894.5.
DR AlphaFoldDB; Q9FLP9; -.
DR BioGRID; 20847; 1.
DR IntAct; Q9FLP9; 1.
DR STRING; 3702.AT5G55120.1; -.
DR PaxDb; Q9FLP9; -.
DR PRIDE; Q9FLP9; -.
DR ProteomicsDB; 221834; -.
DR EnsemblPlants; AT5G55120.1; AT5G55120.1; AT5G55120.
DR GeneID; 835603; -.
DR Gramene; AT5G55120.1; AT5G55120.1; AT5G55120.
DR KEGG; ath:AT5G55120; -.
DR Araport; AT5G55120; -.
DR TAIR; locus:2161620; AT5G55120.
DR eggNOG; KOG2720; Eukaryota.
DR HOGENOM; CLU_041964_1_0_1; -.
DR InParanoid; Q9FLP9; -.
DR OMA; SGACIWL; -.
DR OrthoDB; 1178383at2759; -.
DR PhylomeDB; Q9FLP9; -.
DR BioCyc; MetaCyc:AT5G55120-MON; -.
DR BRENDA; 2.7.7.69; 399.
DR SABIO-RK; Q9FLP9; -.
DR UniPathway; UPA00990; UER00932.
DR PRO; PR:Q9FLP9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLP9; baseline and differential.
DR Genevisible; Q9FLP9; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010475; F:galactose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
DR GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; IDA:TAIR.
DR GO; GO:0080047; F:GDP-L-galactose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0080046; F:quercetin 4'-O-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR InterPro; IPR026506; GDPGP.
DR PANTHER; PTHR20884; PTHR20884; 1.
PE 1: Evidence at protein level;
KW Ascorbate biosynthesis; Cytoplasm; Guanine-nucleotide releasing factor;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..431
FT /note="GDP-L-galactose phosphorylase 2"
FT /id="PRO_0000402542"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Tele-GMP-histidine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 431 AA; 48316 MW; 43119055F345904F CRC64;
MLLKIKRVPT VVSNYQKDET VEEGGCGRNC LSKCCINGAR LPLYTCKNLD KSVGENTESP
VTFLESLVIG EWEDRFQRGL FRYDVTACET KVIPGKYGFI AQLNEGRHLK KRPTEFRVDK
VLQPFDGNKF NFTKVGQEEL LFQFKASTND DDSEIQFLAS MPLDADNSPS VVAINVSPIE
YGHVLLIPRV LDCLPQRIDH KSLLLALQMA AEADNPYFRL GYNSLGAFAT INHLHFQAYY
LAMQFPIEKA SSLKITTTNN GVKISKLLNY PVRGLLVEGG NTIKDLADTV SDASVCLQNN
NIPFNILISD SGKRIFLLPQ CYAEKQALGE VSSTLLDTQV NPAVWEMSGH MVLKRKEDYE
GASEEKAWRL LAEVSLSEER FREVNTMIFD AIGFSSHEEE EEEELEEQNS MNGGSFTIVH
CPSVKEEAVS N
