O59144 (G1PDH_PYRHO) 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:	PH1475

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	346 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.
Sequence caution	The sequence BAA30582.1 differs from that shown. Reason: Erroneous initiation.

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 – 346	346	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		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 [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: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA30582.1. Different initiation.
PIR	F71022.
RefSeq	NP_143340.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O59144.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000002052; EBPYRP00000002052; EBPYRG00000002052.
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
GeneTree	EBGT00050000023171.
HOGENOM	HBG672951.
OMA	DKPALHG.
PhylomeDB	O59144.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	PHOR70601:PH1475-MONOMER.
Family and domain databases
HAMAP	MF_00497_A. G1P_dehydrogenase_A. [Tree]
InterPro	IPR023002. G1P_dehydrogenase_arc. IPR016205. Glycerol_DH. [Graphical view]
KO	K00096.
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:	December 14, 2011
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program