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A4IP94 (G1PDH_GEOTN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:GTNG_1788
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length404 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 probably used for the synthesis of phosphoglycerolipids in Gram-positive bacterial species By similarity. HAMAP MF_00497_B

Catalytic activity

sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497_B

Cofactor

Binds 1 nickel ion per subunit By similarity. HAMAP MF_00497_B

Subunit structure

Homodimer By similarity. HAMAP MF_00497_B

Subcellular location

Cytoplasm Potential HAMAP MF_00497_B.

Sequence similarities

Belongs to the glycerol-1-phosphate dehydrogenase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
NADP
Nickel
   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 – 404404Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_B
PRO_0000350641

Regions

Nucleotide binding117 – 1215NAD By similarity
Nucleotide binding139 – 1424NAD By similarity

Sites

Metal binding1911Nickel; catalytic By similarity
Metal binding2711Nickel; catalytic By similarity
Metal binding2911Nickel; catalytic By similarity
Binding site551NAD By similarity
Binding site1441Substrate By similarity
Binding site1481NAD By similarity
Binding site1911Substrate By similarity
Binding site2751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IP94 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: A30A90E9115BB3B0

FASTA40445,328
        10         20         30         40         50         60 
MNQTLDNIVS LAKQCRGHHH YDISIEQIVV SHEAFNQLAA YLRYKQYKKV VVVADNRTFT 

        70         80         90        100        110        120 
AAGRSLCDKL KNESVLYTVC LIQSDENEDV IADERAIMQV LLETPNDVDA FIAVGAGTVH 

       130        140        150        160        170        180 
DITRFSSYKM KVPFISVPTA PSVDGFTSMG APLIIRGVKK TIQAQAPIAV FADTDVLCQA 

       190        200        210        220        230        240 
PKAMIAAGFG DMVAKYTSLA DWQFAHWMAN EPYCPLVYQL TIQSLNACVD HMEDIAAGNE 

       250        260        270        280        290        300 
KGIHVLMDAL LQSGIAMLLM GQSYSASGAE HHLSHYWEME FLRQNKRQVL HGAKVGVSTP 

       310        320        330        340        350        360 
IIVEHYQRVF WPLLSELKQR PKSMDETIWE RLKIYTDSIQ ELLESLPSPE RIRAMVEKVG 

       370        380        390        400 
GAVAPQQLGI DPLLVERSLK EAHRLRLNRF TMLYCLNECM LMEG

« Hide

References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed: 17372208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NG80-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000557 Genomic DNA. Translation: ABO67148.1.
RefSeqYP_001125893.1. NC_009328.1.

3D structure databases

ProteinModelPortalA4IP94.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4IP94.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4966721.
GenomeReviewsGene locus GTNG_1788 in contig CP000557_GR.
KEGGgtn:GTNG_1788.
NMPDRfig|420246.5.peg.1720.
PATRIC21980041. VBIGeoThe136879_1889.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0371.
HOGENOMHBG313183.
OMAAGFGDMV.
ProtClustDBCLSK873152.

Enzyme and pathway databases

BioCycGTHE420246:GTNG_1788-MONOMER.

Family and domain databases

HAMAPMF_00497_B. G1P_dehydrogenase_B.
[Tree]
InterProIPR023003. G1P_dehydrogenase_bac.
[Graphical view]
KOK02102.
ProtoNetSearch...

Entry information

Entry nameG1PDH_GEOTN
AccessionPrimary (citable) accession number: A4IP94
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: May 1, 2007
Last modified: December 14, 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

SIMILARITY comments

Index of protein domains and families

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