P64186 (GPDA_BRUME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(P)+]
EC=1.1.1.94

Alternative name(s):
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase

Gene names

Name:	gpsA
Ordered Locus Names:	BMEI0174

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP-Rule MF_00394
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP-Rule MF_00394
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate biosynthetic process Inferred from electronic annotation. Source: HAMAP glycerol-3-phosphate catabolic process Inferred from electronic annotation. Source: InterPro glycerophospholipid metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: HAMAP glycerol-3-phosphate dehydrogenase [NAD+] activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 326	326	Glycerol-3-phosphate dehydrogenase [NAD(P)+] HAMAP-Rule MF_00394		PRO_0000137934
Regions
	Nucleotide binding	9 – 14	6	NAD By similarity
	Region	254 – 255	2	Substrate binding By similarity
Sites
	Active site	190	1	Proton acceptor By similarity
	Binding site	107	1	NAD; via amide nitrogen By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	139	1	NAD; via amide nitrogen By similarity
	Binding site	254	1	NAD By similarity
	Binding site	275	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P64186 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 9853E6E4335CA53C	FASTA	326	33,377
	10 20 30 40 50 60 MSTKIAVLGG GAWGTALAAM AAKGGHESWL YARDAETVVA INKDRRNPRY LGDITLADGI 70 80 90 100 110 120 RASTDAAAVV TGADAVLAVI PAQAMRNGLS ELGTLIPQAS PIVLCAKGIE QNTGRLMSEV 130 140 150 160 170 180 VAEILPDHRI AALSGPSFAS DVARGLPTAV TVACEDANTA DRLAALLSGP AFRCYSTTDL 190 200 210 220 230 240 KGVETGGALK NVLAIAAGAA IGRGYGASAQ AALVTRGFAE LRRIGQAMSA RPETIMGLSG 250 260 270 280 290 300 LGDLMLTCSS SQSRNYSYGL ALGRGEDLTS RPLAEGVATA PIAAELCRKH NISAPIIDAV 310 320 GALLDGKITI DEAVTALLNR PLKTED

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008917 Genomic DNA. Translation: AAL51356.1.
PIR	AI3273.
RefSeq	NP_539092.1. NC_003317.1.
3D structure databases
ProteinModelPortal	P64186.
ModBase	Search...
Protein-protein interaction databases
STRING	224914.BMEI0174.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL51356; AAL51356; BMEI0174.
GeneID	1195886.
KEGG	bme:BMEI0174.
PATRIC	17795327. VBIBruMel146950_0027.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000246853.
KO	K00057.
OMA	KGIEHGT.
ProtClustDB	PRK00094.
Enzyme and pathway databases
UniPathway	UPA00940.
Family and domain databases
Gene3D	1.10.1040.10. 1 hit. 3.40.50.720. 1 hit.
HAMAP	MF_00394. NAD_Glyc3P_dehydrog.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR006168. G3P_DH_NAD-dep. IPR006109. G3P_DH_NAD-dep_C. IPR011128. G3P_DH_NAD-dep_N. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11728. PTHR11728. 1 hit.
Pfam	PF07479. NAD_Gly3P_dh_C. 1 hit. PF01210. NAD_Gly3P_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTS	PR00077. GPDHDRGNASE.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPDA_BRUME

Accession

Primary (citable) accession number: P64186
Secondary accession number(s): Q8YJB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program