Q9HS49 (G1PDH_HALSA) Reviewed, UniProtKB/Swiss-Prot

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):
Enantiomeric glycerophosphate synthase
sn-glycerol-1-phosphate dehydrogenase

Gene names

Name:	egsA
Ordered Locus Names:	VNG_0406C

Organism

Halobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)

Taxonomic identifier

64091 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
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 used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea By similarity. HAMAP MF_00497_A
Catalytic activity	sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497_A
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00497_A
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497_A
Subcellular location	Cytoplasm Potential HAMAP MF_00497_A.
Sequence similarities	Belongs to the glycerol-1-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cytoplasm
Ligand	Metal-binding NAD NADP Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycerol-1-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: EC metal 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 – 352	352	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000157340
Regions
	Nucleotide binding	98 – 102	5	NAD By similarity
	Nucleotide binding	120 – 123	4	NAD By similarity
Sites
	Metal binding	172	1	Zinc; catalytic By similarity
	Metal binding	252	1	Zinc; catalytic By similarity
	Metal binding	268	1	Zinc; catalytic By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	129	1	NAD By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	256	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HS49 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 93F3917D26790E15	FASTA	352	36,711
	10 20 30 40 50 60 MFEKSTWIRL PRNVVVGHGV LDDAVEVVRD THLTGRPLVV TSPTPKTVAA ENVVAQFEAV 70 80 90 100 110 120 GDDPAVVVVE EATFNSVERV LGEAEAVDPG YLVGVGGGKA IDIAKLASDH LNVGFVSVPT 130 140 150 160 170 180 AASHDGIVSG RGSVPEGDTR HSVSAAPPLA VIADTGVIAD APWELTTAGC ADIISNYTAV 190 200 210 220 230 240 KDWRLANRLQ HVPYSEYAGA LSQMTAEMLV DNAANIKPEL EESAWVVVKA LVSSGVAMSI 250 260 270 280 290 300 ADSSRPASGS EHLFSHQLDR IAPGKALHGH QVGVGSILAE YLHSGQEGQW MAVRDALASL 310 320 330 340 350 DAPTTADELG VADDEVLAAL TSAHEIRDRY TILGGGISEV AAREAASRTG VI

References

[1]

"Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. , Cruz R., Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P., Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M., Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J., Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L., DasSarma S. Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed: 11016950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE004437 Genomic DNA. Translation: AAG18959.1.
PIR	C84199.
RefSeq	NP_279479.1. NC_002607.1.
3D structure databases
ProteinModelPortal	Q9HS49.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1447263.
GenomeReviews	Gene locus VNG_0406C in contig AE004437_GR.
KEGG	hal:VNG0406C.
NMPDR	fig|64091.1.peg.494.
Phylogenomic databases
HOGENOM	HBG672951.
OMA	CGVGTIM.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	HSP64091:VNG0406C-MONOMER.
Family and domain databases
HAMAP	MF_00497_A. G1P_dehydrogenase_A. [Tree]
InterPro	IPR023002. G1P_dehydrogenase_arc. IPR016205. Glycerol_DH. [Graphical view]
KO	K00096.
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_HALSA

Accession

Primary (citable) accession number: Q9HS49

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	March 1, 2001
Last modified:	November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program