| chain |
|
| checksum |
4BAE83BB932C321A
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| comment |
-
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.CATALYTIC ACTIVITY GDP-alpha-D-mannose = GDP-beta-L-guloseCATALYTIC ACTIVITY GDP-beta-L-gulose = GDP-beta-L-galactoseCOFACTOR Strongly activated by NAD. Activated by NADP. Slightly activated by NADH and NADPH. Inhibited by GDP.BIOPHYSICOCHEMICAL PROPERTIES The catalytic efficiency increases by 2-fold in the presence of NAD(+).PATHWAY Cofactor biosynthesis; L-ascorbate biosynthesis via GDP-alpha-D-mannose pathway; L-ascorbate from GDP-alpha-D-mannose: step 1/5.SUBUNIT Homodimer.SIMILARITY Belongs to the NAD(P)-dependent epimerase/dehydratase family.
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| created |
[InstanceEdit:9682524] Gupta, Parul, 2020-04-08
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| databaseName |
UniProt
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| dbId |
9682499
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| description |
-
recommendedName: GDP-mannose 3,5-epimerase 1 shortName: GDP-Man 3,5-epimerase 1 ecNumber evidence="3"5.1.3.18 alternativeName: OsGME-1
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| displayName |
UniProt:A3C4S4 GME-1
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| geneName |
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GME-1
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Os10g0417600
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LOC_Os10g28200
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OsJ_030296
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OSJNBa0061K21.15
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| identifier |
A3C4S4
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| isSequenceChanged |
false
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| keyword |
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Ascorbate biosynthesis
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Isomerase
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NAD
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Reference proteome
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| modified |
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
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| name |
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| referenceDatabase |
[ReferenceDatabase:2] UniProt
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| schemaClass |
ReferenceGeneProduct
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| secondaryIdentifier |
-
GME1_ORYSJ
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B7EX80
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Q0IXP2
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Q0R4F5
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Q109P5
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Q338B5
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Q5W7P1
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Q8S862
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| sequenceLength |
378
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| species |
[Species:1250427] Oryza sativa subsp. japonica
|
| url |
http://purl.uniprot.org/uniprot/A3C4S4
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