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Q18JW6 (G1PDH_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 47. 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:HQ1560A
OrganismHaloquadratum walsbyi (strain DSM 16790) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloquadratum

Protein attributes

Sequence length348 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 – 348348Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_1000050601

Regions

Nucleotide binding94 – 985NAD By similarity
Nucleotide binding116 – 1194NAD By similarity

Sites

Metal binding1681Zinc; catalytic By similarity
Metal binding2481Zinc; catalytic By similarity
Metal binding2641Zinc; catalytic By similarity
Binding site1211Substrate By similarity
Binding site1251NAD By similarity
Binding site1681Substrate By similarity
Binding site2521Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q18JW6 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 6CFF9077B6120D75

FASTA34836,477
        10         20         30         40         50         60 
MLKKTTWIKL PRNVLVGHDV IGDLAAAIEE LYLDGRPLIV TSPTPDQLIG NRVRSQFADP 

        70         80         90        100        110        120 
QTVSVDHASF DAVEAVIDTA KATDAGYLIG LGGGKPIDTA KMASDRLGCG FVSVPTAASH 

       130        140        150        160        170        180 
DGIVSGRSSI PEGDTRHSVA ADPPLAVVAD TAVLAEAPWE LTTAGCADII SNYTAVKDWQ 

       190        200        210        220        230        240 
LAHRLQDVEY SEYAGALSQM TAEMLVDNSD AIKQGFEESA WLVAKALVSS GVAMSIAGSS 

       250        260        270        280        290        300 
RPASGAEHLI SHQLDRLVPD AALHGHQVGV ASIVTAYLHT GENGEWEDIR AALADVGAPT 

       310        320        330        340 
TATELGIDEE IFIQAITSAH AIRDRHTILG NGVSEAAARE AAVFTDVC

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed: 16820047] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM180088 Genomic DNA. Translation: CAJ51688.1.
RefSeqYP_657330.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18JW6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ18JW6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4194032.
GenomeReviewsGene locus HQ1560A in contig AM180088_GR.
KEGGhwa:HQ1560A.
NMPDRfig|362976.6.peg.564.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMACGVGTIM.
PhylomeDBQ18JW6.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycHWAL362976:HQ1560A-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_HALWD
AccessionPrimary (citable) accession number: Q18JW6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: November 16, 2011
This is version 47 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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