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GDP-L-galactose phosphorylase 2 (EC 2.7.7.69) (Protein VITAMIN C DEFECTIVE 5)

 GGAP2_ARATH             Reviewed;         431 AA.
Q9FLP9;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 101.
RecName: Full=GDP-L-galactose phosphorylase 2;
EC=2.7.7.69;
AltName: Full=Protein VITAMIN C DEFECTIVE 5;
Name=VTC5; Synonyms=VTC2L; OrderedLocusNames=At5g55120;
ORFNames=MCO15.7;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
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).
[5]
FUNCTION, INDUCTION BY LIGHT, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
[6]
IDENTIFICATION, AND FUNCTION.
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).
[7]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
[8]
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).
-!- 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:17485667, ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094}.
-!- CATALYTIC ACTIVITY: GDP-L-galactose + phosphate = alpha-L-
galactose 1-phosphate + GDP. {ECO:0000269|PubMed:18463094}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.0083 mM for GDP-L-galactose {ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094};
KM=0.012 mM for GDP-D-glucose {ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094};
KM=1.3 mM for GDP-D-mannose {ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094};
KM=1.0 mM for phosphate {ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094};
KM=0.22 mM for phosphate {ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094};
KM=16 mM for L-galactose 1-phosphate
{ECO:0000269|PubMed:17877701, ECO:0000269|PubMed:18463094};
KM=10 mM for D-glucose 1-phosphate {ECO:0000269|PubMed:17877701,
ECO:0000269|PubMed:18463094};
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.;
-!- 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. Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flowers and
siliques. {ECO:0000269|PubMed:17877701}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: No visible phenotype and slightly decreased
ascorbate levels; due to the partial redundancy with VTC2. 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}.
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EMBL; AB010071; BAB08581.1; -; Genomic_DNA.
EMBL; CP002688; AED96583.1; -; Genomic_DNA.
EMBL; AY063788; AAL36095.1; -; mRNA.
EMBL; AY091285; AAM14224.1; -; mRNA.
RefSeq; NP_200323.1; NM_124894.5.
UniGene; At.21005; -.
ProteinModelPortal; Q9FLP9; -.
BioGrid; 20847; 1.
IntAct; Q9FLP9; 1.
STRING; 3702.AT5G55120.1; -.
PaxDb; Q9FLP9; -.
EnsemblPlants; AT5G55120.1; AT5G55120.1; AT5G55120.
GeneID; 835603; -.
Gramene; AT5G55120.1; AT5G55120.1; AT5G55120.
KEGG; ath:AT5G55120; -.
Araport; AT5G55120; -.
TAIR; locus:2161620; AT5G55120.
eggNOG; KOG2720; Eukaryota.
eggNOG; ENOG4111FR6; LUCA.
HOGENOM; HOG000006065; -.
InParanoid; Q9FLP9; -.
KO; K14190; -.
OMA; DYNDASE; -.
OrthoDB; EOG09360ACA; -.
PhylomeDB; Q9FLP9; -.
BioCyc; MetaCyc:AT5G55120-MONOMER; -.
BRENDA; 2.7.7.69; 399.
SABIO-RK; Q9FLP9; -.
UniPathway; UPA00990; UER00932.
PRO; PR:Q9FLP9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FLP9; baseline and differential.
Genevisible; Q9FLP9; 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:0080047; F:GDP-L-galactose phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0080046; F:quercetin 4'-O-glucosyltransferase activity; IDA:TAIR.
GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
GO; GO:0010193; P:response to ozone; 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 1 431 GDP-L-galactose phosphorylase 2.
/FTId=PRO_0000402542.
COMPBIAS 357 407 Glu-rich.
ACT_SITE 235 235 Tele-GMP-histidine intermediate.
{ECO:0000250}.
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


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