P43798 (GPDA_HAEIN) 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:	HI_0605

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

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 Reference 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_0000137969
Regions
	Nucleotide binding	12 – 17	6	NAD By similarity
	Region	259 – 260	2	Substrate binding By similarity
Sites
	Active site	195	1	Proton acceptor By similarity
	Binding site	110	1	NAD; via amide nitrogen By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	143	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)
	P43798 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4913F8F2203B7CFC	FASTA	335	36,394
	10 20 30 40 50 60 MITSQTPITV LGAGSYGTAL AITFSRNGSP THLWGHNPAH IAQMQTERQN YRFLPDVIFP 70 80 90 100 110 120 EDLHLESNLA QAMEYSQDIL IVVPSHAFGE ILIKIKPHLK AHHRLIWATK GLERNTGRLL 130 140 150 160 170 180 QTVVEEQLGT QYPLAVLSGP TFAKELAQGL PSAITLAANN EQFAREFQSR IHCSKGFRVY 190 200 210 220 230 240 INSDMTGVQL GGAIKNVIAI GAGISDGMGF GANARTALIT RGIAEITRLG ISLGANTNTF 250 260 270 280 290 300 MGMSGLGDLV LTCTDNQSRN RRFGLMLGKG LDAQMAMENI GQVVEGFYNT KEAYLLAQRQ 310 320 330 GVEMPITEQI YQMLFCGKSA QDVAISLLGR ACKGE

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22264.1.
PIR	F64080.
RefSeq	NP_438763.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P43798.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0605.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22264; AAC22264; HI_0605.
GeneID	949436.
KEGG	hin:HI0605.
PATRIC	20189789. VBIHaeInf48452_0629.
Phylogenomic databases
eggNOG	COG0240.
KO	K00057.
OMA	DVIGCEI.
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_HAEIN

Accession

Primary (citable) accession number: P43798

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program