Reviewed, UniProtKB/Swiss-Prot O59144 (G1PDH_PYRHO)

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:	PH1475

Organism

Pyrococcus horikoshii [Complete proteome] [HAMAP]

Taxonomic identifier

53953 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	346 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
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 – 346	346	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000157350
Regions
	Nucleotide binding	93 – 97	5	NAD By similarity
	Nucleotide binding	115 – 118	4	NAD By similarity
Sites
	Metal binding	167	1	Zinc; catalytic By similarity
	Metal binding	247	1	Zinc; catalytic By similarity
	Metal binding	263	1	Zinc; catalytic By similarity
	Binding site	120	1	Substrate By similarity
	Binding site	124	1	NAD By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	251	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O59144-1 [UniParc]. Last modified August 2, 2002. Version 2. Checksum: AF961F022DA16863	FASTA	346	37,371
	10 20 30 40 50 60 MHLMEFPREV ILGKNLIQEI NNVIKRLKLG SPGLVVYGPI TKKIAGSNVE KIVKEEFEVY 70 80 90 100 110 120 SITVKEAHIN EVERVISKIR DKGIKWAIAV GGGSIIDVTK LASFKMGIPF ISFPTTASHD 130 140 150 160 170 180 GIASANASIK GLNVKTSIKA KPPIAVIADI DVIKTAPKRY LAAGVGDIVS NITAVRDWKL 190 200 210 220 230 240 AHKLKGEYFS EYAASLSLMS AKMVIRDAEI IRLGQDEGIR KVVKALISSG VAMSIAGSSR 250 260 270 280 290 300 PASGAEHLFS HALDMLLDKP ALHGEQTGIG TIIMAYLHGI NWKKIRDTLK IVGAPTTAYE 310 320 330 340 LGIDPEIIIE ALTIAHTIRP ERYTILGKEG ITREAAEKAA KITGVI

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OT3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000001 Genomic DNA. Translation: BAA30582.1. Different initiation.
PIR	F71022.
RefSeq	NP_143340.1.
3D structure databases
HSSP	HSSP built from PDB template 1JQA based on UniProtKB P32816.
ModBase	Search...
Genome annotation databases
GeneID	1443794.
GenomeReviews	Gene locus PH1475 in contig BA000001_GR.
KEGG	pho:PH1475.
NMPDR	fig|70601.1.peg.1447.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O59144.
OMA	YTAVLDW.
Enzyme and pathway databases
BRENDA	1.1.1.261. 74679.
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_PYRHO

Accession

Primary (citable) accession number: O59144

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	August 2, 2002
Last modified:	November 3, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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