Reviewed, UniProtKB/Swiss-Prot Q65GC3 (G1PDH_BACLD)

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
Synonyms:	araM
Ordered Locus Names:	BLi03025, BL00349

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential.
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 – 401	401	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000350638
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	57	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)
	Q65GC3-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 9B12132EEDC26E61	FASTA	401	43,198
	10 20 30 40 50 60 MNDLISYVKK TLGACECGTV HHPLTVEKIA IGDNAVEQEL PAFVKSASYK KAAVIYDETT 70 80 90 100 110 120 GRLAGKRIAS LLEETAETVP VLLEANEAGD VTADEQTLVS ALIGVPIDAD VLIAAGAGTI 130 140 150 160 170 180 HDIVRFCAYQ RGIPFISVPT APSVDGFTSA GAPLILKGKK QTVQTTAPIA LFADLELLCQ 190 200 210 220 230 240 APQNMVAAGF GDMLGKVTSL ADWEISRLLA GEPYCPAASR LTREALDQCL DRKDDIAAKM 250 260 270 280 290 300 RDGIEKLMES LILSGLVMLV LDHSRPASGG EHHLSHYLEM KALENNKRQV LHGAKVGCSA 310 320 330 340 350 360 IMLTDIYRSL IGASLGDQHA EQAIRSVYEK LPDGKKMAEW MRRIGGPVSF KELDVEEELV 370 380 390 400 REALAYAHQL RDRYTGLKII NQYGLLPGLL GKGPGVKGVK M

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000002 Genomic DNA. Translation: AAU24532.1. AE017333 Genomic DNA. Translation: AAU41891.1.
RefSeq	YP_080170.1. YP_092584.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q65GC3.
Genome annotation databases
GeneID	3028655. 3098580.
GenomeReviews	Gene locus BLi03025 in contig AE017333_GR. Gene locus BL00349 in contig CP000002_GR.
KEGG	bld:BLi03025. bli:BL00349.
NMPDR	fig|279010.5.peg.3373.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q65GC3.
OMA	LHGAKVG.
Family and domain databases
HAMAP	MF_00497. [Tree]
InterPro	IPR002658. DHQ_synth_AroB. [Graphical view]
Pfam	PF01761. DHQ_synthase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G1PDH_BACLD

Accession

Primary (citable) accession number: Q65GC3
Secondary accession number(s): Q62RS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 33 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)