Reviewed, UniProtKB/Swiss-Prot Q9KBR3 (G1PDH_BACHD)

Names and origin

Protein names

Recommended name:
    Glycerol-1-phosphate dehydrogenase [NAD(P)+]
      Short name=G1P dehydrogenase
      Short name=G1PDH
    EC=1.1.1.261
Alternative name(s):
    sn-glycerol-1-phosphate dehydrogenase
    Enantiomeric glycerophosphate synthase

Gene names

Name:	egsA
Ordered Locus Names:	BH1862

Organism

Bacillus halodurans [Complete proteome] [HAMAP]

Taxonomic identifier

86665 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Inferred 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
Catalytic activity	sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497
Cofactor	Binds 1 nickel ion per subunit By similarity. HAMAP MF_00497
Subunit structure	Homodimer By similarity. HAMAP MF_00497
Subcellular location	Cytoplasm Potential HAMAP MF_00497.
Sequence similarities	Belongs to the glycerol-1-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cytoplasm
Ligand	Metal-binding NAD NADP Nickel
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-dehydroquinate synthase activity Inferred from electronic annotation. Source: InterPro glycerol-1-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: HAMAP nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 399	399	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000350637
Regions
	Nucleotide binding	118 – 122	5	NAD By similarity
	Nucleotide binding	140 – 143	4	NAD By similarity
Sites
	Metal binding	192	1	Nickel; catalytic By similarity
	Metal binding	272	1	Nickel; catalytic By similarity
	Metal binding	292	1	Nickel; catalytic By similarity
	Binding site	56	1	NAD By similarity
	Binding site	145	1	Substrate By similarity
	Binding site	149	1	NAD By similarity
	Binding site	192	1	Substrate By similarity
	Binding site	276	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KBR3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: EAFE42EB49629D73	FASTA	399	43,585
	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

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 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB05581.1.
PIR	F83882.
RefSeq	NP_242728.1.
3D structure databases
SMR	Q9KBR3. Positions 23-388.
ModBase	Search...
Genome annotation databases
GeneID	890490.
GenomeReviews	Gene locus BH1862 in contig BA000004_GR.
KEGG	bha:BH1862.
NMPDR	fig|272558.1.peg.1862.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG313183.
OMA	HISHWIE.
Enzyme and pathway databases
BioCyc	BHAL272558:BH1862-MONOMER.
Family and domain databases
HAMAP	MF_00497_B. G1P_dehydrogenase_B. [Tree]
InterPro	IPR002658. DHQ_synth_AroB. [Graphical view]
Pfam	PF01761. DHQ_synthase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G1PDH_BACHD

Accession

Primary (citable) accession number: Q9KBR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	October 1, 2000
Last modified:	January 19, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)