Q2R1V8 (GME2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GDP-mannose 3,5-epimerase 2
Short name=GDP-Man 3,5-epimerase 2
EC=5.1.3.18

Gene names

Name:	GME-2
Ordered Locus Names:	Os11g0591100, LOC_Os11g37890

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes a reversible epimerization of GDP-D-mannose that precedes the committed step in the biosynthesis of vitamin C (L-ascorbate), resulting in the hydrolysis of the highly energetic glycosyl-pyrophosphoryl linkage. Able to catalyze 2 distinct epimerization reactions and can release both GDP-L-galactose and GDP-L-gulose from GDP-mannose By similarity.
Catalytic activity	GDP-mannose = GDP-L-galactose.
Cofactor	NAD By similarity.
Pathway	Cofactor biosynthesis; L-ascorbate biosynthesis via GDP-alpha-D-mannose pathway; L-ascorbate from GDP-alpha-D-mannose: step 1/5. Ref.3
Sequence similarities	Belongs to the sugar epimerase family.
Sequence caution	The sequence ABA94523.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence ABA94524.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AK102348 differs from that shown. Reason: Erroneous termination at position 156. Translated as Glu.

Ontologies

Keywords
Biological process	Ascorbate biosynthesis
Ligand	NAD
Molecular function	Isomerase
Gene Ontology (GO)
Biological process	L-ascorbic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GDP-mannose 3,5-epimerase activity Inferred from electronic annotation. Source: EC coenzyme binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 371	371	GDP-mannose 3,5-epimerase 2		PRO_0000233698
Regions
	Nucleotide binding	29 – 55	27	NAD By similarity
	Region	138 – 140	3	Substrate binding By similarity
	Region	210 – 212	3	Substrate binding By similarity
	Region	235 – 237	3	Substrate binding By similarity
Sites
	Active site	168	1	Proton acceptor By similarity
	Binding site	53	1	NAD By similarity
	Binding site	73	1	NAD By similarity
	Binding site	98	1	Substrate; via carbonyl oxygen By similarity
	Binding site	168	1	NAD By similarity
	Binding site	172	1	NAD By similarity
	Binding site	197	1	Substrate By similarity
	Binding site	219	1	Substrate By similarity
	Binding site	300	1	Substrate By similarity
	Binding site	350	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2R1V8 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: 628597B74842A2E5	FASTA	371	42,132
	10 20 30 40 50 60 MALNEEYTYV ELEKEPYWPF EKLRISITGA GGFIASHIAR RLKSEGHYII ASDWKKNEHM 70 80 90 100 110 120 TEDMFCHEFH LVDLRVMDNC LKVTTGVDHV FNLAADMGGM GFIQSNHSVI MYNNTMISFN 130 140 150 160 170 180 MLEAARINGV KRFFYASSAC IYPEFKQLDT VVSLKESDAW PAEPQDAYGL EKLATEELCK 190 200 210 220 230 240 HYTKDFGIEC RVGRFHNIYG PFGTWKGGRE KAPAAFCRKA LTSTDRFEMW GDGLQTRSFT 250 260 270 280 290 300 FIDECVEGVL RLTKSDFREP VNIGSDEMVS MNEMAEIVLS FENKQLPIHH IPGPEGVRGR 310 320 330 340 350 360 NSDNTLIKEK LGWAPTMRLK DGLRITYFWI KEQLEKEKAE GVDLSAYGSS KVVQTQAPVQ 370 LGSLRAADGK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications." The rice chromosomes 11 and 12 sequencing consortia BMC Biol. 3:20-20(2005) [PubMed: 16188032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[2]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed: 12869764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.
[3]	"The biosynthetic pathway of vitamin C in higher plants." Wheeler G.L., Jones M.A., Smirnoff N. Nature 393:365-369(1998) [PubMed: 9620799] [Abstract] Cited for: PATHWAY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DP000010 Genomic DNA. Translation: ABA94522.1. DP000010 Genomic DNA. Translation: ABA94523.1. Sequence problems. DP000010 Genomic DNA. Translation: ABA94524.1. Sequence problems. AK102348 mRNA. No translation available.
RefSeq	NP_001068183.1. NM_001074715.1.
UniGene	Os.10082.
3D structure databases
ProteinModelPortal	Q2R1V8.
SMR	Q2R1V8. Positions 7-369.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2R1V8.
Proteomic databases
PRIDE	Q2R1V8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os11g37890.1; LOC_Os11g37890.1; LOC_Os11g37890.
GeneID	4350816.
KEGG	osa:4350816.
Organism-specific databases
Gramene	Q2R1V8.
Phylogenomic databases
GeneTree	EPGT00070000029761.
OMA	IDDCVEG.
PhylomeDB	Q2R1V8.
ProtClustDB	PLN02695.
Family and domain databases
InterPro	IPR001509. Epimerase_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GME2_ORYSJ

Accession

Primary (citable) accession number: Q2R1V8
Secondary accession number(s): Q2R1V9, Q2R1W0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	May 2, 2006
Last modified:	December 14, 2011
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program