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Q8U147 (G1PDH_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 64. 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:PF1382
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [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.

Sequence caution

The sequence AAL81506.1 differs from that shown. Reason: Erroneous initiation.

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 – 346346Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157349

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
Q8U147 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: 74879F173ED94048

FASTA34637,345
        10         20         30         40         50         60 
MHIMEFPREV ILGKNVISET VNVAKRLSFS SPVLVVYGPK TKEIAGKDVE RVLKEEFDVH 

        70         80         90        100        110        120 
SVIVKEATIN EVEKVEGIIR DNKVKWAIAV GGGTIIDVTK LASYRAGIPF VSFPTTASHD 

       130        140        150        160        170        180 
GIASANASIK GLGTKTSIKA RPPVAVIADI RIIKSAPRRY LAAGVGDVIS NITAVRDWKL 

       190        200        210        220        230        240 
AHKIKGEYFS EYAAALSLMS AKMVMRDAEI IRIGDDEGVR KVVKALISSG VAMSIAGSSR 

       250        260        270        280        290        300 
PASGAEHLFS HALDLLLEKP ALHGEQTGIG TIIMAYLHGI NWRKIKETLQ KVGAPTTAYE 

       310        320        330        340 
LGVDPEIIIE ALTIAHTIRP ERYTILGRDG LTREAAERAA KITGVI

« Hide

References

[1]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009950 Genomic DNA. Translation: AAL81506.1. Different initiation.
RefSeqNP_579111.1. NC_003413.1.

3D structure databases

ProteinModelPortalQ8U147.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000004361; EBPYRP00000004222; EBPYRG00000004361.
GeneID1469258.
GenomeReviewsGene locus PF1382 in contig AE009950_GR.
KEGGpfu:PF1382.
NMPDRfig|186497.1.peg.1429.

Phylogenomic databases

GeneTreeEBGT00050000023171.
HOGENOMHBG672951.
OMAADWELAH.
PhylomeDBQ8U147.
ProtClustDBPRK00843.

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_PYRFU
AccessionPrimary (citable) accession number: Q8U147
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: December 14, 2011
This is version 64 of the entry and version 2 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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