Q146B6 (GPDA_BURXL) 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:	Bxeno_A0285
ORF Names:	Bxe_A4177

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia xenovorans

Protein attributes

Sequence length	335 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 – 335	335	Glycerol-3-phosphate dehydrogenase [NAD(P)+] HAMAP-Rule MF_00394		PRO_0000255292
Regions
	Nucleotide binding	10 – 15	6	NAD By similarity
	Region	259 – 260	2	Substrate binding By similarity
Sites
	Active site	195	1	Proton acceptor By similarity
	Binding site	111	1	NAD; via amide nitrogen By similarity
	Binding site	111	1	Substrate By similarity
	Binding site	144	1	NAD; via amide nitrogen By similarity
	Binding site	259	1	NAD By similarity
	Binding site	285	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q146B6 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 135DD59A96BBBF22	FASTA	335	34,413
	10 20 30 40 50 60 MPAMKVAVLG AGAWGTALAG HLAVRHDTVL WARQPALIAD LRASHENARY LAGVALPPAL 70 80 90 100 110 120 RYETDLNAAL DHALADNALC VVATPVAGLR GLFRAMRDAG KVPAHVVWLC KGFEADSQLM 130 140 150 160 170 180 PHQVVAAELP EHGSNGVLSG PSFAREVGQG LPVALTIASA SAACRERTVA AFHHGAMRIY 190 200 210 220 230 240 TGDDVVGVEV GGAVKNVLAI ATGIADGLGL GLNARAALIT RGLAEMSRLG VTLGGRAETF 250 260 270 280 290 300 TGLTGLGDLI LTATGDLSRN RTVGLQLAAG RTLDDILGGL GHVAEGVRCA QAVLAIARAH 310 320 330 AIEMPITQAV CAVLFDGVAP RDAVSALLRR DSKAE

References

[1]

"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M. Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LB400.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000270 Genomic DNA. Translation: ABE28823.1.
RefSeq	YP_556875.1. NC_007951.1.
3D structure databases
ProteinModelPortal	Q146B6.
ModBase	Search...
Protein-protein interaction databases
STRING	266265.Bxe_A4177.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABE28823; ABE28823; Bxe_A4177.
GeneID	4001861.
KEGG	bxe:Bxe_A4177.
PATRIC	19325921. VBIBurXen52548_0302.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0240.
HOGENOM	HOG000246853.
KO	K00057.
OMA	DVIGCEI.
ProtClustDB	PRK00094.
Enzyme and pathway databases
BioCyc	BXEN266265:GJII-290-MONOMER.
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.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
PROSITE	PS00957. NAD_G3PDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GPDA_BURXL

Accession

Primary (citable) accession number: Q146B6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	August 22, 2006
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program