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Q8ZWP5 (G1PDH_PYRAE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 65. 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:PAE1685
OrganismPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Taxonomic identifier178306 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length342 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

Subunit structure

Homodimer By similarity. 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 – 342342Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000157348

Regions

Nucleotide binding84 – 885NAD By similarity
Nucleotide binding106 – 1094NAD By similarity

Sites

Metal binding1601Zinc; catalytic By similarity
Metal binding2411Zinc; catalytic By similarity
Metal binding2601Zinc; catalytic By similarity
Binding site1111Substrate By similarity
Binding site1151NAD By similarity
Binding site1601Substrate By similarity
Binding site2451Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZWP5 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 5E6811B6CCD133DB

FASTA34236,878
        10         20         30         40         50         60 
MKQLESFQIP RIVIFGPGAI LKTPLVVSEL KAGRILVISG KSATTAYANQ VAQLLSNYSV 

        70         80         90        100        110        120 
DVVRYNEVDL SKSSYDLVIG VGGGRPIDMA KVYSCVHKKP LVVIPTAASH DGIASPYVSY 

       130        140        150        160        170        180 
TLSQKLQTYG KIVASPVAII ADTSVILSAP SRLLKAGIGD LLGKIIAVRD WQLAHRLKGE 

       190        200        210        220        230        240 
EYSEYAAHLA VTSYKIAATN ARRIRNFTRE EDVRVLVKAL IGCGVAMGIA GSSRPCSGSE 

       250        260        270        280        290        300 
HLFAHAIELR LQEESSEAVH GELVALGTII MAYLHGINWR RIKKIAEIVG LPTTLKQAGI 

       310        320        330        340 
DADMAVEALT TAHALRPDRY TILGNGLSRE AARRALEDTE LI

« Hide

References

[1]"Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed: 11792869] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE009441 Genomic DNA. Translation: AAL63655.1.
RefSeqNP_559473.1. NC_003364.1.

3D structure databases

ProteinModelPortalQ8ZWP5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1465904.
GenomeReviewsGene locus PAE1685 in contig AE009441_GR.
KEGGpai:PAE1685.
NMPDRfig|178306.1.peg.1163.

Phylogenomic databases

HOGENOMHBG672951.
OMAAIHGELV.
ProtClustDBCLSK899668.

Enzyme and pathway databases

BioCycPAER178306:PAE1685-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_PYRAE
AccessionPrimary (citable) accession number: Q8ZWP5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 1, 2002
Last modified: December 14, 2011
This is version 65 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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