O25614 (GPDA_HELPY) 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:	HP_0961

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	312 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 – 312	312	Glycerol-3-phosphate dehydrogenase [NAD(P)+] HAMAP-Rule MF_00394		PRO_0000137971
Regions
	Nucleotide binding	7 – 12	6	NAD By similarity
	Region	241 – 242	2	Substrate binding By similarity
Sites
	Active site	177	1	Proton acceptor By similarity
	Binding site	95	1	NAD; via amide nitrogen By similarity
	Binding site	95	1	Substrate By similarity
	Binding site	127	1	NAD; via amide nitrogen By similarity
	Binding site	241	1	NAD By similarity
	Binding site	267	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O25614 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 5786864D43E8D266	FASTA	312	33,392
	10 20 30 40 50 60 MEIAVFGGGA WGRALAFAFG EKNEVKIISR RDLNEPLKKL NDALISKGSA PIEQVDLQRG 70 80 90 100 110 120 LKATLYVIAI SVQHLREWFQ NASLPKNAKV LIASKGIEVL NKAFVSEIAK DFIDPNSLCF 130 140 150 160 170 180 LAGPSFAAEI IQGLPCALVI HSNNQALALE FANKTPSFIR AYAQQDIIGG EIAGAYKNVI 190 200 210 220 230 240 AIAGGVCDGL KLGNSAKASL LSRGLVEMQR FGAFFGGKTE TFLGLSGAGD LFLTANSILS 250 260 270 280 290 300 RNYRVGLGLA QNKPLEVVLE ELGEVAEGVK TTNAIVEIAR KYGIYTPIAS ELALLLKGKS 310 VLESMNDLIR RA

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD08003.1.
PIR	A64640.
RefSeq	NP_207753.1. NC_000915.1. YP_006934878.1. NC_018939.1.
3D structure databases
ProteinModelPortal	O25614.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3377N.
MINT	MINT-175509.
STRING	85962.HP0961.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD08003; AAD08003; HP_0961.
GeneID	13870154. 899494.
KEGG	heo:C694_04950. hpy:HP0961.
PATRIC	20593235. VBIHelPyl33062_0999.
Phylogenomic databases
eggNOG	COG0240.
KO	K00057.
OMA	KHEMEEV.
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_HELPY

Accession

Primary (citable) accession number: O25614

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program