Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9KBR3 (G1PDH_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BH1862
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length399 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 – 399399Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_B
PRO_0000350637

Regions

Nucleotide binding118 – 1225NAD By similarity
Nucleotide binding140 – 1434NAD By similarity

Sites

Metal binding1921Nickel; catalytic By similarity
Metal binding2721Nickel; catalytic By similarity
Metal binding2921Nickel; catalytic By similarity
Binding site561NAD By similarity
Binding site1451Substrate By similarity
Binding site1491NAD By similarity
Binding site1921Substrate By similarity
Binding site2761Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KBR3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EAFE42EB49629D73

FASTA39943,585
        10         20         30         40         50         60 
MNHLLKQAKR VASECECGHE HQWIEMDELQ LGRNAINYLP EYLHEKGLLH VTIVADANTY 

        70         80         90        100        110        120 
AVAGQLVAQL LKGRGIDVEN CILKEQGALT LLADEHGLGQ LVIGAAKETD VFLAVGAGTI 

       130        140        150        160        170        180 
HDLTRIASYK FGKPFIAIPT APSVDGFTSM GAPVIRDGVK ITFQTQAPIA LFADLDFLTQ 

       190        200        210        220        230        240 
APRSMVAAGF GDMLGKSTSL VDWQVSHMLN DEPFCPAVFH MTKSALTMCM EHADEIAACN 

       250        260        270        280        290        300 
EQGIRLLTEA LIMSGLAMLI FGHSHPASGA EHHLSHYWEM AFLRSGGTQP LHGAKVGYAT 

       310        320        330        340        350        360 
MLISALYKNE ARKKIETFQG EGSPLVNSIH KHRERLLMLI DTIPESSDIQ RLLESVGGAV 

       370        380        390 
KSADLALADS LEDEALEKAH KLRERCTLLY CLNEHLKTS

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000004 Genomic DNA. Translation: BAB05581.1.
PIRF83882.
RefSeqNP_242728.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KBR3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000053488; EBBACP00000052127; EBBACG00000053479.
GeneID890490.
GenomeReviewsGene locus BH1862 in contig BA000004_GR.
KEGGbha:BH1862.
NMPDRfig|272558.1.peg.1862.
PATRIC18940854. VBIBacHal18977_1940.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001321.
HOGENOMHBG313183.
OMANTHRIAG.
ProtClustDBCLSK873152.

Enzyme and pathway databases

BioCycBHAL272558:BH1862-MONOMER.

Family and domain databases

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

Entry information

Entry nameG1PDH_BACHD
AccessionPrimary (citable) accession number: Q9KBR3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 55 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents