GME1_ORYSI
ID GME1_ORYSI Reviewed; 378 AA.
AC A2Z7B3; Q0IXP2; Q0R4F5; Q109P5; Q338B5; Q5W7P1; Q8S862;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=GDP-mannose 3,5-epimerase 1;
DE Short=GDP-Man 3,5-epimerase 1;
DE EC=5.1.3.18 {ECO:0000250|UniProtKB:Q93VR3};
DE AltName: Full=OsGME-1;
GN ORFNames=OsI_032456;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Panicle;
RA Wang F., Wang H., Wang J.;
RT "An epimerase/dehydratase gene from rice panicle shorter than 3cm.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP PATHWAY.
RX PubMed=9620799; DOI=10.1038/30728;
RA Wheeler G.L., Jones M.A., Smirnoff N.;
RT "The biosynthetic pathway of vitamin C in higher plants.";
RL Nature 393:365-369(1998).
CC -!- FUNCTION: Catalyzes a reversible epimerization of GDP-D-mannose that
CC precedes the committed step in the biosynthesis of vitamin C (L-
CC ascorbate), resulting in the hydrolysis of the highly energetic
CC glycosyl-pyrophosphoryl linkage. Able to catalyze 2 distinct
CC epimerization reactions and can release both GDP-L-galactose and GDP-L-
CC gulose from GDP-mannose. {ECO:0000250|UniProtKB:Q93VR3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose = GDP-beta-L-gulose; Xref=Rhea:RHEA:63800,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:149550; EC=5.1.3.18;
CC Evidence={ECO:0000250|UniProtKB:Q93VR3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-gulose = GDP-beta-L-galactose;
CC Xref=Rhea:RHEA:63804, ChEBI:CHEBI:61454, ChEBI:CHEBI:149550;
CC EC=5.1.3.18; Evidence={ECO:0000250|UniProtKB:Q93VR3};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q93VR3};
CC -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via GDP-alpha-
CC D-mannose pathway; L-ascorbate from GDP-alpha-D-mannose: step 1/5.
CC {ECO:0000269|PubMed:9620799}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; DQ119303; ABA18619.1; -; mRNA.
DR EMBL; CM000135; EAY78497.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Z7B3; -.
DR SMR; A2Z7B3; -.
DR STRING; 39946.A2Z7B3; -.
DR PRIDE; A2Z7B3; -.
DR EnsemblPlants; BGIOSGA032923-TA; BGIOSGA032923-PA; BGIOSGA032923.
DR Gramene; BGIOSGA032923-TA; BGIOSGA032923-PA; BGIOSGA032923.
DR HOGENOM; CLU_007383_4_2_1; -.
DR OMA; QTATDKF; -.
DR UniPathway; UPA00990; UER00931.
DR Proteomes; UP000007015; Chromosome 10.
DR GO; GO:0047918; F:GDP-mannose 3,5-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05273; GME-like_SDR_e; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR033890; GDP-Man_epi.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Ascorbate biosynthesis; Isomerase; NAD; Reference proteome.
FT CHAIN 1..378
FT /note="GDP-mannose 3,5-epimerase 1"
FT /id="PRO_0000295026"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 36..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242..244
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 93
FT /note="S -> G (in Ref. 1; ABA18619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42808 MW; 4D62CF3F5729220B CRC64;
MGSSEKNGTA YGEYTYAELE REQYWPSEKL RISITGAGGF IGSHIARRLK SEGHYIIASD
WKKNEHMTED MFCHEFHLVD LRVMDNCLKV TNSVDHVFNL AADMGGMGFI QSNHSVIMYN
NTMISFNMLE AARINGVKRF FYASSACIYP EFKQLETNVS LKESDAWPAE PQDAYGLEKL
ATEELCKHYT KDFGIECRVG RFHNIYGPFG TWKGGREKAP AAFCRKAQTS TDRFEMWGDG
LQTRSFTFID ECVEGVLRLT KSDFREPVNI GSDEMVSMNE MAEIILSFED RELPIHHIPG
PEGVRGRNSD NTLIKEKLGW APTMKLKDGL RFTYFWIKEQ IEKEKTQGVD IAGYGSSKVV
STQAPVQLGS LRAADGKE
