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A7Z7G4 (G1PDH_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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
Synonyms:araM
Ordered Locus Names:RBAM_025820
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length394 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 – 394394Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_B
PRO_0000350636

Regions

Nucleotide binding116 – 1205NAD By similarity
Nucleotide binding138 – 1414NAD By similarity

Sites

Metal binding1901Nickel; catalytic By similarity
Metal binding2701Nickel; catalytic By similarity
Metal binding2901Nickel; catalytic By similarity
Binding site541NAD By similarity
Binding site1431Substrate By similarity
Binding site1471NAD By similarity
Binding site1901Substrate By similarity
Binding site2741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z7G4 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: CBBDB52DBBCA522D

FASTA39442,473
        10         20         30         40         50         60 
MKRSPEDIQS EFDKEGASRS PIQIEDIVIG ANAKEELLRF LQKKCWNHPV IVCDRNTYEA 

        70         80         90        100        110        120 
AGRLLADELR AGGIKASKVI IPEHEAGAAA ADERTLVYTL INLAEETDVI IAAGAGTIHD 

       130        140        150        160        170        180 
ITRFAAYQRG LPFISFPTAP SVDGFTSAGA PLILNGIKTT IQTKAPIALF ADTNVLKEAP 

       190        200        210        220        230        240 
RSMTAAGFGD MLGKITSLAD WEISRRLAGE PYSEAGAKLV KDALWQCIDH RAAIAMGTEA 

       250        260        270        280        290        300 
GIQILMEALI VSGLVMLALD HSRPASGGEH HISHWIEMEM LKAKQPPILH GAKVGCACAV 

       310        320        330        340        350        360 
LSDTYKELAC HEKLAELPPH FREAIQSAYE GLPDGKTIAG WLASAGGPAC FDEIGVKQDL 

       370        380        390 
VSDALKHAHT LRDRYTGLTI INENAALFAH HLHQ

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000560 Genomic DNA. Translation: ABS74940.1.
RefSeqYP_001422171.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z7G4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z7G4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000006880; EBBACP00000006758; EBBACG00000006872.
GeneID5462378.
GenomeReviewsGene locus RBAM_025820 in contig CP000560_GR.
KEGGbay:RBAM_025820.
PATRIC18750292. VBIBacAmy31356_2619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0371.
GeneTreeEBGT00050000001321.
HOGENOMHBG313183.
OMATITDICK.
ProtClustDBCLSK873152.

Enzyme and pathway databases

BioCycBAMY326423:RBAM_025820-MONOMER.

Family and domain databases

HAMAPMF_00497_B. G1P_dehydrogenase_B.
[Tree]
InterProIPR023003. G1P_dehydrogenase_bac.
[Graphical view]
KOK00096.
ProtoNetSearch...

Entry information

Entry nameG1PDH_BACA2
AccessionPrimary (citable) accession number: A7Z7G4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 36 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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