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Q9V0V0 (G1PDH_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol-1-phosphate dehydrogenase [NAD(P)+]
Short name=G1P dehydrogenase
Short name=G1PDH
EC=1.1.1.261
Alternative name(s):
Enantiomeric glycerophosphate synthase
sn-glycerol-1-phosphate dehydrogenase
Gene names
Name:egsA
Ordered Locus Names:PYRAB06890
ORF Names:PAB1907
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol-1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea By similarity. HAMAP MF_00497_A

Catalytic activity

sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497_A

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00497_A

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497_A

Subcellular location

Cytoplasm Potential HAMAP MF_00497_A.

Sequence similarities

Belongs to the glycerol-1-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycerol-1-phosphate dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157347

Regions

Nucleotide binding93 – 975NAD By similarity
Nucleotide binding115 – 1184NAD By similarity

Sites

Metal binding1671Zinc; catalytic By similarity
Metal binding2471Zinc; catalytic By similarity
Metal binding2631Zinc; catalytic By similarity
Binding site1201Substrate By similarity
Binding site1241NAD By similarity
Binding site1671Substrate By similarity
Binding site2511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V0V0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 1553DE1561E23DC8

FASTA34637,414
        10         20         30         40         50         60 
MHLMEFPREV ILGKNLVPEV NNVIKRLKLE SPGLVVYGPV TKKIAGESVK KAIRDEFDVY 

        70         80         90        100        110        120 
SITVKKAHIG EVEKVEAKIR DYNIKWAIAV GGGSIIDVTK LASYRSGIPF ISFPTTASHD 

       130        140        150        160        170        180 
GIASANASIR GIEAKTSIKA RPPIAVIADI EVIKTAPRRY LAAGVGDVIS NITAVRDWKL 

       190        200        210        220        230        240 
AHKLKGEYFS EYAAALSLMS AKMVIRDAEI IRLGNDEGVR KVIKALISSG VAMSIAGSSR 

       250        260        270        280        290        300 
PASGAEHLFS HALDLLLDKP ALHGEQTGIG TIIMAYLHGI NWRKIKETLK TVGAPTSAYE 

       310        320        330        340 
LGIDPEIIIE ALTIAHKIRP ERYTILGKEG LTREAAEKAA KITGVI

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ248285 Genomic DNA. Translation: CAB49603.1.
PIRB75111.
RefSeqNP_126372.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V0V0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000002593; EBPYRP00000002524; EBPYRG00000002593.
GeneID1495593.
GenomeReviewsGene locus PYRAB06890 in contig AL096836_GR.
KEGGpab:PAB1907.
NMPDRfig|272844.1.peg.717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000023171.
HOGENOMHBG672951.
OMADKPALHG.
PhylomeDBQ9V0V0.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycPABY272844:PAB1907-MONOMER.

Family and domain databases

HAMAPMF_00497_A. G1P_dehydrogenase_A.
[Tree]
InterProIPR023002. G1P_dehydrogenase_arc.
IPR016205. Glycerol_DH.
[Graphical view]
KOK00096.
PIRSFPIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG1PDH_PYRAB
AccessionPrimary (citable) accession number: Q9V0V0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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