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A1RZJ9 (G1PDH_THEPD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 38. 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:Tpen_1231
OrganismThermofilum pendens (strain Hrk 5)
Taxonomic identifier368408 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermofilaceae › Thermofilum

Protein attributes

Sequence length347 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 – 347347Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A
PRO_0000350663

Regions

Nucleotide binding90 – 945NAD By similarity
Nucleotide binding112 – 1154NAD By similarity

Sites

Metal binding1651Zinc; catalytic By similarity
Metal binding2451Zinc; catalytic By similarity
Metal binding2621Zinc; catalytic By similarity
Binding site1171Substrate By similarity
Binding site1211NAD By similarity
Binding site1651Substrate By similarity
Binding site2491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1RZJ9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: A06DF0E00A2C68D8

FASTA34736,660
        10         20         30         40         50         60 
MRAELPKRVV VERGALQFLP EVLRELGCSK TVVVTDSGVW SVVGSVVEGA LRGLAYEVVY 

        70         80         90        100        110        120 
IEAADNSNVE RARSAARRVE ACAVAGLGGG RPVDVAKYAA FMEGLPFVSV PTAISHDGFA 

       130        140        150        160        170        180 
SPIVALKDPE GNPLSIFTRP PAAVLVDLAV VSRAPRRLLA SGVGDIVGKV TSVADARLAQ 

       190        200        210        220        230        240 
RLTGEEVPEV ALRMAETAAR MVLDEVDEIA SWTERGVGVL AQAGLLAGMA MAVAGSSRPC 

       250        260        270        280        290        300 
SGSEHLFSHS LDKYVPWKKS LHGEQVGVGA IIASYLHGFN WRVIRDALAK VGAPTTVEGL 

       310        320        330        340 
GVTGEDAVRA LLKARELRKR FTILDVVELN EGLAWKVLRE TGVAPTA

« Hide

References

[1]"Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction."
Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B. expand/collapse author list , Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.
J. Bacteriol. 190:2957-2965(2008) [PubMed: 18263724] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hrk 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000505 Genomic DNA. Translation: ABL78629.1.
RefSeqYP_920632.1. NC_008698.1.

3D structure databases

ProteinModelPortalA1RZJ9.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1RZJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4601163.
GenomeReviewsGene locus Tpen_1231 in contig CP000505_GR.
KEGGtpe:Tpen_1231.

Phylogenomic databases

eggNOGarNOG04488.
HOGENOMHBG672951.
OMADKPALHG.
PhylomeDBA1RZJ9.

Enzyme and pathway databases

BioCycTPEN368408:TPEN_1231-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_THEPD
AccessionPrimary (citable) accession number: A1RZJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: February 6, 2007
Last modified: November 16, 2011
This is version 38 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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