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B0R3A6 (G1PDH_HALS3) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. 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:OE1602F
OrganismHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) [Complete proteome] [HAMAP]
Taxonomic identifier478009 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length352 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 – 352352Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350644

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
B0R3A6 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 93F3917D26790E15

FASTA35236,711
        10         20         30         40         50         60 
MFEKSTWIRL PRNVVVGHGV LDDAVEVVRD THLTGRPLVV TSPTPKTVAA ENVVAQFEAV 

        70         80         90        100        110        120 
GDDPAVVVVE EATFNSVERV LGEAEAVDPG YLVGVGGGKA IDIAKLASDH LNVGFVSVPT 

       130        140        150        160        170        180 
AASHDGIVSG RGSVPEGDTR HSVSAAPPLA VIADTGVIAD APWELTTAGC ADIISNYTAV 

       190        200        210        220        230        240 
KDWRLANRLQ HVPYSEYAGA LSQMTAEMLV DNAANIKPEL EESAWVVVKA LVSSGVAMSI 

       250        260        270        280        290        300 
ADSSRPASGS EHLFSHQLDR IAPGKALHGH QVGVGSILAE YLHSGQEGQW MAVRDALASL 

       310        320        330        340        350 
DAPTTADELG VADDEVLAAL TSAHEIRDRY TILGGGISEV AAREAASRTG VI

« Hide

References

[1]"Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
Genomics 91:335-346(2008) [PubMed: 18313895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29341 / DSM 671 / R1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM774415 Genomic DNA. Translation: CAP13220.1.
RefSeqYP_001688569.1. NC_010364.1.

3D structure databases

ProteinModelPortalB0R3A6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0R3A6.

Proteomic databases

PRIDEB0R3A6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5952519.
GenomeReviewsGene locus OE1602F in contig AM774415_GR.
KEGGhsl:OE1602F.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG672951.
OMACGVGTIM.
PhylomeDBB0R3A6.
ProtClustDBPRK00843.

Enzyme and pathway databases

BioCycHSAL478009:OE1602F-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_HALS3
AccessionPrimary (citable) accession number: B0R3A6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: April 8, 2008
Last modified: December 14, 2011
This is version 34 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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