Reviewed, UniProtKB/Swiss-Prot Q18JW6 (G1PDH_HALWD)

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

Gene names

Name:	egsA
Ordered Locus Names:	HQ1560A

Organism

Haloquadratum walsbyi (strain DSM 16790) [Complete proteome] [HAMAP]

Taxonomic identifier

362976 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloquadratum

Protein attributes

Sequence length	348 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
Catalytic activity	sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00497
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497
Subcellular location	Cytoplasm Potential HAMAP MF_00497.
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	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-dehydroquinate synthase activity Inferred from electronic annotation. Source: InterPro glycerol-1-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: HAMAP zinc 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 – 348	348	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_1000050601
Regions
	Nucleotide binding	94 – 98	5	NAD By similarity
	Nucleotide binding	116 – 119	4	NAD By similarity
Sites
	Metal binding	168	1	Zinc; catalytic By similarity
	Metal binding	248	1	Zinc; catalytic By similarity
	Metal binding	264	1	Zinc; catalytic By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	NAD By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	252	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q18JW6-1 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: 6CFF9077B6120D75	FASTA	348	36,477
	10 20 30 40 50 60 MLKKTTWIKL PRNVLVGHDV IGDLAAAIEE LYLDGRPLIV TSPTPDQLIG NRVRSQFADP 70 80 90 100 110 120 QTVSVDHASF DAVEAVIDTA KATDAGYLIG LGGGKPIDTA KMASDRLGCG FVSVPTAASH 130 140 150 160 170 180 DGIVSGRSSI PEGDTRHSVA ADPPLAVVAD TAVLAEAPWE LTTAGCADII SNYTAVKDWQ 190 200 210 220 230 240 LAHRLQDVEY SEYAGALSQM TAEMLVDNSD AIKQGFEESA WLVAKALVSS GVAMSIAGSS 250 260 270 280 290 300 RPASGAEHLI SHQLDRLVPD AALHGHQVGV ASIVTAYLHT GENGEWEDIR AALADVGAPT 310 320 330 340 TATELGIDEE IFIQAITSAH AIRDRHTILG NGVSEAAARE AAVFTDVC

References

[1]

"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity." Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D. BMC Genomics 7:169-169(2006) [PubMed: 16820047] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM180088 Genomic DNA. Translation: CAJ51688.1.
RefSeq	YP_657330.1.
3D structure databases
SMR	Q18JW6. Positions 5-342.
ModBase	Search...
Protein-protein interaction databases
STRING	Q18JW6.
Genome annotation databases
GeneID	4194032.
GenomeReviews	Gene locus HQ1560A in contig AM180088_GR.
KEGG	hwa:HQ1560A.
NMPDR	fig|362976.6.peg.564.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	KWMQLPR.
PhylomeDB	Q18JW6.
Enzyme and pathway databases
BioCyc	HWAL362976:HQ1560A-MONOMER.
Family and domain databases
HAMAP	MF_00497_A. G1P_dehydrogenase_A. [Tree]
InterPro	IPR002658. DHQ_synth_AroB. IPR016205. Glycerol_DH. [Graphical view]
Pfam	PF01761. DHQ_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_HALWD

Accession

Primary (citable) accession number: Q18JW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	July 25, 2006
Last modified:	January 19, 2010
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)