GME2_ORYSJ
ID GME2_ORYSJ Reviewed; 371 AA.
AC Q2R1V8; A0A0P0Y3W9; Q0IRW9; Q2R1V9; Q2R1W0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=GDP-mannose 3,5-epimerase 2;
DE Short=GDP-Man 3,5-epimerase 2;
DE EC=5.1.3.18 {ECO:0000250|UniProtKB:Q93VR3};
GN Name=GME-2;
GN OrderedLocusNames=Os11g0591100 {ECO:0000312|EMBL:BAF28546.1},
GN LOC_Os11g37890 {ECO:0000312|EMBL:ABA94522.1};
GN ORFNames=OsJ_34492 {ECO:0000312|EMBL:EAZ18955.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
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 -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA94523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABA94524.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AK102348; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; DP000010; ABA94522.1; -; Genomic_DNA.
DR EMBL; DP000010; ABA94523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000010; ABA94524.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008217; BAF28546.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT14673.1; -; Genomic_DNA.
DR EMBL; CM000148; EAZ18955.1; -; Genomic_DNA.
DR EMBL; AK102348; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015617577.1; XM_015762091.1.
DR AlphaFoldDB; Q2R1V8; -.
DR SMR; Q2R1V8; -.
DR STRING; 4530.OS11T0591100-01; -.
DR PaxDb; Q2R1V8; -.
DR PRIDE; Q2R1V8; -.
DR EnsemblPlants; Os11t0591100-01; Os11t0591100-01; Os11g0591100.
DR GeneID; 4350816; -.
DR Gramene; Os11t0591100-01; Os11t0591100-01; Os11g0591100.
DR KEGG; osa:4350816; -.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_2_1; -.
DR InParanoid; Q2R1V8; -.
DR OMA; RSFMYID; -.
DR OrthoDB; 662484at2759; -.
DR UniPathway; UPA00990; UER00931.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000007752; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR Genevisible; Q2R1V8; OS.
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..371
FT /note="GDP-mannose 3,5-epimerase 2"
FT /id="PRO_0000233698"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138..140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210..212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 371 AA; 42132 MW; 628597B74842A2E5 CRC64;
MALNEEYTYV ELEKEPYWPF EKLRISITGA GGFIASHIAR RLKSEGHYII ASDWKKNEHM
TEDMFCHEFH LVDLRVMDNC LKVTTGVDHV FNLAADMGGM GFIQSNHSVI MYNNTMISFN
MLEAARINGV KRFFYASSAC IYPEFKQLDT VVSLKESDAW PAEPQDAYGL EKLATEELCK
HYTKDFGIEC RVGRFHNIYG PFGTWKGGRE KAPAAFCRKA LTSTDRFEMW GDGLQTRSFT
FIDECVEGVL RLTKSDFREP VNIGSDEMVS MNEMAEIVLS FENKQLPIHH IPGPEGVRGR
NSDNTLIKEK LGWAPTMRLK DGLRITYFWI KEQLEKEKAE GVDLSAYGSS KVVQTQAPVQ
LGSLRAADGK E
