A1RV58 (G1PDH_PYRIL) 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:	Pisl_1689

Organism

Pyrobaculum islandicum (strain DSM 4184 / JCM 9189) [Complete proteome] [HAMAP]

Taxonomic identifier

384616 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length	342 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
Subunit structure	Homodimer By similarity. HAMAP MF_00497_A
Subcellular location	Cytoplasm Potential HAMAP MF_00497_A.
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	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 – 342	342	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_1000050608
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)
	A1RV58 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 9164C9A2FBF4DC09	FASTA	342	37,155
	10 20 30 40 50 60 MKQLESFEIP RTVIFGPGAI SKIHQIVASQ KASKILIITG RSVTLQYAKT IADMLTDRSV 70 80 90 100 110 120 EVLRYDYIDI EKSGFDLVLG VGGGRPIDMA KVYSYVHKKP LVIVPTSASH DGIASPYVSY 130 140 150 160 170 180 TLAQKMIKYG KIMASPIAIV ADTSIILNAP SRLLKAGVGD LLGKIIAVRD WKLAHRLKGE 190 200 210 220 230 240 EYSEYASHLS LTSYRIVVAN AARIKNFVRE EDVRVLVKAL IGCGVAMGIA GSSRPCSGSE 250 260 270 280 290 300 HLFAHAIEIR LEESGGDAIH GELVALGTII MAYLHGINWR RVKKIAKLVG LPTTLREAGI 310 320 330 340 DYDLAIEALV VAHTLRPDRY TILGDGLSKD AARRAIEATE LA

References

[1]

"Complete sequence of Pyrobaculum islandicum DSM 4184." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 4184 / JCM 9189.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000504 Genomic DNA. Translation: ABL88840.1.
RefSeq	YP_931183.1. NC_008701.1.
3D structure databases
ProteinModelPortal	A1RV58.
ModBase	Search...
Protein-protein interaction databases
STRING	A1RV58.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4618030.
GenomeReviews	Gene locus Pisl_1689 in contig CP000504_GR.
KEGG	pis:Pisl_1689.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	AIHGELV.
PhylomeDB	A1RV58.
ProtClustDB	CLSK899668.
Enzyme and pathway databases
BioCyc	PISL384616:PISL_1689-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_PYRIL

Accession

Primary (citable) accession number: A1RV58

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program