Reviewed, UniProtKB/Swiss-Prot A8ABP9 (G1PDH_IGNH4)

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:	Igni_1174

Organism

Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125) [Complete proteome] [HAMAP]

Taxonomic identifier

453591 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Ignicoccus

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential.
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 – 352	352	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000350646
Regions
	Nucleotide binding	97 – 101	5	NAD By similarity
	Nucleotide binding	119 – 122	4	NAD By similarity
Sites
	Metal binding	171	1	Zinc; catalytic By similarity
	Metal binding	251	1	Zinc; catalytic By similarity
	Metal binding	267	1	Zinc; catalytic By similarity
	Binding site	124	1	Substrate By similarity
	Binding site	128	1	NAD By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	255	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8ABP9-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 7FD9612CC30CF2C9	FASTA	352	38,031
	10 20 30 40 50 60 MRDRHEIELM KRVVVGRGTR RELPKVIKAL GFDGGEVLVV TGPHVWSEWG DELQGLLEKE 70 80 90 100 110 120 GFKVDFVTVV EPSVEEANKV LEGLNGEPNV VVGFGGGKAI DVAKYVAMKL GRDVVSVPTA 130 140 150 160 170 180 TSHDGIASPF SSLKGLKGPT SVKTKTPIAV VADIEVIARA PERLNRAGIG DVLAKFSAVR 190 200 210 220 230 240 DWRLAHVLKG EYYGSYAASL ALMSAKHVLK YSPLLKALSE DGLRILVEAL ISSGVAMCIA 250 260 270 280 290 300 GSSRPASGSE HLFSHALDVI ANRPALHGEQ VGVGTIMMLY LHGSKLWRKV RKVLRDLNLP 310 320 330 340 350 TTAEELGVED EKIIEALTIA HKIRPERYTI LGSDGLTREA AERLARTTGV IK

References

[1]

"Unicellular symbiosis at high temperature: genomic insights into the Ignicoccus hospitalis - Naoarchaeum equitans relationship." Podar M., Anderson I., Ivanova N., Wall M., Mavrommatis K., Lykidis A., Chen J., Hudson M., Deciu C., Hutchison D., Eads J., Fernandes F., Tamang D., Szeto E., Land M., Lapidus A., Kyrpides N., Chang C. , Saier M., Eisen J., Rachel R., Huber H., Keller M., Richardson P., Stetter K. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000816 Genomic DNA. Translation: ABU82351.1.
RefSeq	YP_001435758.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8ABP9.
Genome annotation databases
GeneID	5561731.
GenomeReviews	Gene locus Igni_1174 in contig CP000816_GR.
KEGG	iho:Igni_1174.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	YTAVLDW.
Family and domain databases
HAMAP	MF_00497. [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_IGNH4

Accession

Primary (citable) accession number: A8ABP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 19 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)