ID   GME2_ORYSJ              Reviewed;         371 AA.
AC   Q2R1V8; Q2R1V9; Q2R1W0;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=GDP-mannose 3,5-epimerase 2;
DE            Short=GDP-Man 3,5-epimerase 2;
DE            EC=5.1.3.18;
GN   Name=GME-2; OrderedLocusNames=Os11g0591100, LOC_Os11g37890;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
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
RT   resistance genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=22752273; 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   [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
CC       that precedes the committed step in the biosynthesis of vitamin C
CC       (L-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
CC       GDP-L-gulose from GDP-mannose (By similarity).
CC   -!- CATALYTIC ACTIVITY: GDP-mannose = GDP-L-galactose.
CC   -!- COFACTOR: NAD (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbic acid biosynthesis via
CC       GDP-D-mannose pathway; L-ascorbic acid from GDP-D-mannose: step
CC       1/5.
CC   -!- SIMILARITY: Belongs to the sugar epimerase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABA94523.1; Type=Erroneous gene model prediction;
CC       Sequence=ABA94524.1; Type=Erroneous gene model prediction;
CC       Sequence=AK102348; Type=Erroneous termination; Positions=156; Note=Translated as Glu;
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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; AK102348; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001068183.1; -.
DR   UniGene; Os.10082; -.
DR   SMR; Q2R1V8; 8-369.
DR   GeneID; 4350816; -.
DR   KEGG; osa:4350816; -.
DR   Gramene; Q2R1V8; -.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0047918; F:GDP-mannose 3,5-epimerase activity; IEA:EC.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01370; Epimerase; 1.
PE   2: Evidence at transcript level;
KW   Ascorbate biosynthesis; Isomerase; NAD.
FT   CHAIN         1    371       GDP-mannose 3,5-epimerase 2.
FT                                /FTId=PRO_0000233698.
FT   NP_BIND      29     55       NAD (By similarity).
FT   REGION      138    140       Substrate binding (By similarity).
FT   REGION      210    212       Substrate binding (By similarity).
FT   REGION      235    237       Substrate binding (By similarity).
FT   ACT_SITE    168    168       Proton acceptor (By similarity).
FT   BINDING      53     53       NAD (By similarity).
FT   BINDING      73     73       NAD (By similarity).
FT   BINDING      98     98       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     168    168       NAD (By similarity).
FT   BINDING     172    172       NAD (By similarity).
FT   BINDING     197    197       Substrate (By similarity).
FT   BINDING     219    219       Substrate (By similarity).
FT   BINDING     300    300       Substrate (By similarity).
FT   BINDING     350    350       Substrate (By similarity).
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
//