Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5JH91 (G1PDH_PYRKO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:TK0789
OrganismPyrococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Thermococcus kodakaraensis (strain KOD1))
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length351 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
Reference 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 – 351351Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157351

Regions

Nucleotide binding98 – 1025NAD By similarity
Nucleotide binding120 – 1234NAD By similarity

Sites

Metal binding1721Zinc; catalytic By similarity
Metal binding2521Zinc; catalytic By similarity
Metal binding2681Zinc; catalytic By similarity
Binding site1251Substrate By similarity
Binding site1291NAD By similarity
Binding site1721Substrate By similarity
Binding site2561Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JH91 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 67A8EC4FEA4F15F0

FASTA35137,756
        10         20         30         40         50         60 
MERRIHLMQL PREVLLGENL TGEVVSVAKR IGLTGKALVI YGPKTKEIAG RDVEDAIKSA 

        70         80         90        100        110        120 
YEVSSLTIRK GATMEEVERT IEKIKDEGIG WVIAVGGGSI IDVAKLSSFK TGVPFISFPT 

       130        140        150        160        170        180 
TASHDGIASA NASIKDLGSK TSVKAVPPVA VIADVKVIKT APYRYLAAGV GDTISNLTAV 

       190        200        210        220        230        240 
RDWQLAHRIK GEYYSEYAAS LSLMSAKMVM RNADIIRLGN EESVRKVIKA LISTGVAMSI 

       250        260        270        280        290        300 
AGSSRPASGA EHLFSHALDM LLDKPALHGE QTGLGTIIMA YLHGMKWERV RETLKRVGAP 

       310        320        330        340        350 
TNAYELGIDP EVIIEALTIA HTIRPERYTI LGKDGLTREA AEKAAKITGV I 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed: 15710748] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD84978.1.
RefSeqYP_183202.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JH91.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000006418; EBPYRP00000006199; EBPYRG00000006417.
GeneID3235756.
GenomeReviewsGene locus TK0789 in contig AP006878_GR.
KEGGtko:TK0789.
NMPDRfig|69014.3.peg.1149.

Phylogenomic databases

eggNOGarNOG04488.
GeneTreeEBGT00050000023171.
HOGENOMHBG672951.
OMADKPALHG.
PhylomeDBQ5JH91.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycTKOD69014:TK0789-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_PYRKO
AccessionPrimary (citable) accession number: Q5JH91
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: November 16, 2011
This is version 58 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