A3MTM6 (G1PDH_PYRCJ) 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:	Pcal_0566

Organism

Pyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]

Taxonomic identifier

410359 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length	338 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 – 338	338	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_1000050607
Regions
	Nucleotide binding	81 – 85	5	NAD By similarity
	Nucleotide binding	103 – 106	4	NAD By similarity
Sites
	Metal binding	157	1	Zinc; catalytic By similarity
	Metal binding	238	1	Zinc; catalytic By similarity
	Metal binding	256	1	Zinc; catalytic By similarity
	Binding site	108	1	Substrate By similarity
	Binding site	112	1	NAD By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	242	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3MTM6 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: CBB439BAEFEEB468	FASTA	338	36,990
	10 20 30 40 50 60 MKKVERFEVP RTIIFGPGAL EKTPEVIPPS GRVLIITGKS STRKYAERVA ELLKQNCEII 70 80 90 100 110 120 SYDQVELEKP GFDLVIGIGG GRPLDMAKVY SYIHKKPFVA IPTSASHDGI ASPYVSFSLT 130 140 150 160 170 180 QRFSKYGKIS SSPVAIIADT SIILSAPSRL LKAGIGDLLG KIIAVRDWQL AHRLKGEEYS 190 200 210 220 230 240 EYAAHLSLTS YKIAVGNAQK IKNFIREEDV RVLVKALIGC GVAMGIAGSS RPCSGSEHLF 250 260 270 280 290 300 AHAIEVRVEK EDEVVHGELV ALGTIIMAYL HGINWRRIKR IADIIGLPTS LRQANIDVDL 310 320 330 ALEALTTAHT LRPDRYTILG DGLSREAAKR ALEDVELI

References

[1]

"Complete sequence of Pyrobaculum calidifontis JCM 11548." 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., Mikhailova N. , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCM 11548 / VA1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000561 Genomic DNA. Translation: ABO07993.1.
RefSeq	YP_001055459.1. NC_009073.1.
3D structure databases
ProteinModelPortal	A3MTM6.
ModBase	Search...
Protein-protein interaction databases
STRING	A3MTM6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4910242.
GenomeReviews	Gene locus Pcal_0566 in contig CP000561_GR.
KEGG	pcl:Pcal_0566.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	CGVGTIM.
PhylomeDB	A3MTM6.
ProtClustDB	CLSK899668.
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_PYRCJ

Accession

Primary (citable) accession number: A3MTM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program