A6URL4 (G1PDH_METVS) 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:	Mevan_1239

Organism

Methanococcus vannielii (strain SB / ATCC 35089 / DSM 1224) [Complete proteome] [HAMAP]

Taxonomic identifier

406327 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length	334 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.

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 – 334	334	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000350659
Regions
	Nucleotide binding	77 – 81	5	NAD By similarity
	Nucleotide binding	99 – 102	4	NAD By similarity
Sites
	Metal binding	147	1	Zinc; catalytic By similarity
	Metal binding	225	1	Zinc; catalytic By similarity
	Metal binding	246	1	Zinc; catalytic By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	108	1	NAD By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6URL4 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 310DB6F1E2BF9183	FASTA	334	37,018
	10 20 30 40 50 60 MIVIPRYSLI KEKASERLPE LLENLNLKKP LVITGKNTKK YSKGFEFIYY DEIDIYNEEG 70 80 90 100 110 120 FQKIGKEYDS IIGIGGGKPI DIGKIISNKS KKPFVSVPTT ASNDGIASPI VSLTQPSYLA 130 140 150 160 170 180 ESPIAIVADI DIIRESPKKL LSAGMGDIVS NITAVLDWEL GKIEMNEKYS DSSGIFSKTI 190 200 210 220 230 240 AIELIDYVLN YDLKEYPKKL VKSLIGSGIS IAIAHSSRPA SGSEHLFSHA LDNLKNKYEL 250 260 270 280 290 300 NINSLHGEQC GLGTIIISQM YYEEGRIDFK TVEKVKNSLK AVNAPVTGKK LGFDEDLLIE 310 320 330 ALSSAHKVRK RHTILRNGLS KEKAREILEK SEII

References

[1]

"Complete sequence of Methanococcus vannielii SB." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. , Sieprawska-Lupa M., Whitman W.B., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SB / ATCC 35089 / DSM 1224.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000742 Genomic DNA. Translation: ABR55136.1.
RefSeq	YP_001323748.1. NC_009634.1.
3D structure databases
ProteinModelPortal	A6URL4.
ModBase	Search...
Protein-protein interaction databases
STRING	A6URL4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5324937.
GenomeReviews	Gene locus Mevan_1239 in contig CP000742_GR.
KEGG	mvn:Mevan_1239.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	CGVGTIM.
ProtClustDB	CLSK876301.
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_METVS

Accession

Primary (citable) accession number: A6URL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	August 21, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program