Reviewed, UniProtKB/Swiss-Prot B1YCY7 (G1PDH_THENV)

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:	Tneu_0711

Organism

Thermoproteus neutrophilus (strain DSM 2338 / JCM 9278 / V24Sta) [Complete proteome] [HAMAP]

Taxonomic identifier

444157 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Thermoproteus

Protein attributes

Sequence length	342 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 – 342	342	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000350662
Regions
	Nucleotide binding	84 – 88	5	NAD By similarity
	Nucleotide binding	106 – 109	4	NAD By similarity
Sites
	Metal binding	160	1	Zinc; catalytic By similarity
	Metal binding	241	1	Zinc; catalytic By similarity
	Metal binding	260	1	Zinc; catalytic By similarity
	Binding site	111	1	Substrate By similarity
	Binding site	115	1	NAD By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	245	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1YCY7-1 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: C75634FE8AF756A8	FASTA	342	36,475
	10 20 30 40 50 60 MKQLESFEIP RTVVFGPGAI LKIPDIVSGL RVGKVLIISG KSATQQYAKT VASLLSGYSA 70 80 90 100 110 120 EILKYDEVEL EKSGFDLIIG VGGGRPLDMA KVYSYVHKRP LIVVPTSASH DGIASPYISY 130 140 150 160 170 180 ILAEKVKRYG KVVASPIAIV ADTSIILSAP RRLLRAGVGD LLGKVVAVRD WQLAHRLKGE 190 200 210 220 230 240 EYSEYAALLS LSSYRIVVAN AGKIGNFVRE EDVRALVKAL IGCGVAMGIA GSSRPCSGSE 250 260 270 280 290 300 HLFAHAIERR LEGAEGEAIH GELVALGAIV MAYLHGINWR RIKKAAGAVG LPTTLKQAGI 310 320 330 340 DLDLAIEALT TAHTLRPDRY TILGDGLSAS AARKALEDTE LI

References

[1]

"Complete sequence of Thermoproteus neutrophilus V24Sta." Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M., Saltikov C., House C.H., Richardson P. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP001014 Genomic DNA. Translation: ACB39650.1.
RefSeq	YP_001794096.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6165664.
GenomeReviews	Gene locus Tneu_0711 in contig CP001014_GR.
KEGG	tne:Tneu_0711.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	ADWELAH.
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_THENV

Accession

Primary (citable) accession number: B1YCY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	May 20, 2008
Last modified:	November 3, 2009
This is version 16 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)