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Information on EC 1.1.1.95 - phosphoglycerate dehydrogenase

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IUBMB Comments
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase .
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This record set is specific for:
UNIPROT: O58256
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
phgdh, phosphoglycerate dehydrogenase, 3-phosphoglycerate dehydrogenase, d-3-phosphoglycerate dehydrogenase, 3-pgdh, 3pgdh, pgdh3, pgdh1, ehpgdh, d-phosphoglycerate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD-dependent D-3-phosphoglycerate dehydrogenase
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3-PGDH
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3-phosphoglycerate dehydrogenase
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3-phosphoglyceric acid dehydrogenase
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A10
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alpha-phosphoglycerate dehydrogenase
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D-3-phosphoglycerate dehydrogenase
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D-3-phosphoglycerate:NAD oxidoreductase
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dehydrogenase, phosphoglycerate
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glycerate 3-phosphate dehydrogenase
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glycerate-1,3-phosphate dehydrogenase
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PGDH
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phosphoglycerate oxidoreductase
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phosphoglyceric acid dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
3-phospho-D-glycerate:NAD+ 2-oxidoreductase
This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9075-29-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O58256_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
333
0
38048
TrEMBL
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures is determined using X-ray diffraction to resolution of 1.95 A, crystals are grown at room temperature by sitting-drop method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kumar, S.M.; Pampa, K.J.; Manjula, M.; Hemantha Kumar, G.; Kunishima, N.; Lokanath, N.K.
Crystal structures of type IIIH NAD-dependent D-3-phosphoglycerate dehydrogenase from two thermophiles
Biochem. Biophys. Res. Commun.
451
126-130
2014
Pyrococcus horikoshii (O58256), Pyrococcus horikoshii, Sulfurisphaera tokodaii (Q972A9), Sulfurisphaera tokodaii, Pyrococcus horikoshii DSM 12428 (O58256)
Manually annotated by BRENDA team