Q5V5G2 (G1PDH_HALMA) 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:	rrnAC0175

Organism

Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

272569 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

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
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_1000050600
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)
	Q5V5G2 [UniParc]. Last modified December 7, 2004. Version 1. Checksum: DCE40115A55A3E02	FASTA	352	37,198
	10 20 30 40 50 60 MFEKRTWIRL PRNVVVGHGV LGQTIEAVSE LHLTGRPLVV SSPTPHDVAG KQVVAQFEDE 70 80 90 100 110 120 GYDPSEIVIE EASFDAVQQV IDHASDIDAG FLLGVGGGKA IDITKMAADD LGLGFVSVPT 130 140 150 160 170 180 AASHDGIVSG RGSVPEGDTR HSVAAEPPLA VIADTEVLAE APWRLTTAGC ADIISNYTAV 190 200 210 220 230 240 RDWQLAHRLK NVHYSEYAGA LSQMTAEMLV ESADSIKQGL EESSWIVVKA LVSSGVAMSI 250 260 270 280 290 300 ADSSRPASGA EHLFSHQLDR LVPDGALHGH QVGVGSIMTE YLHSGQKGKW RDARDALAAI 310 320 330 340 350 GAPTTADELG IDDETVIEAL TTAHQIRDRY TVLGDGMSEE AAIEAATVTG VI

References

[1]

"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed: 15520287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY596297 Genomic DNA. Translation: AAV45240.1.
RefSeq	YP_134946.1. NC_006396.1.
3D structure databases
HSSP	HSSP built from PDB template 1JPU based on UniProtKB P32816.
ProteinModelPortal	Q5V5G2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3129920.
GenomeReviews	Gene locus rrnAC0175 in contig AY596297_GR.
KEGG	hma:rrnAC0175.
NMPDR	fig|272569.1.peg.199.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG672951.
OMA	CGVGTIM.
PhylomeDB	Q5V5G2.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	HMAR272569:RRNAC0175-MONOMER.
Family and domain databases
HAMAP	MF_00497_A. G1P_dehydrogenase_A. [Tree]
InterPro	IPR023002. G1P_dehydrogenase_arc. IPR016205. Glycerol_DH. [Graphical view]
KO	K00005. K00096.
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_HALMA

Accession

Primary (citable) accession number: Q5V5G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 7, 2004
Last modified:	December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program