A0B5P3 (G1PDH_METTP) 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:	Mthe_0219

Organism

Methanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]

Taxonomic identifier

349307 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosaetaceae › Methanosaeta

Protein attributes

Sequence length	354 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 – 354	354	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000350658
Regions
	Nucleotide binding	102 – 106	5	NAD By similarity
	Nucleotide binding	124 – 127	4	NAD By similarity
Sites
	Metal binding	176	1	Zinc; catalytic By similarity
	Metal binding	256	1	Zinc; catalytic By similarity
	Metal binding	272	1	Zinc; catalytic By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	133	1	NAD By similarity
	Binding site	176	1	Substrate By similarity
	Binding site	260	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0B5P3 [UniParc]. Last modified November 28, 2006. Version 1. Checksum: 722AC0A554357CEE	FASTA	354	37,335
	10 20 30 40 50 60 MLRMRTRSAS WMELPRRVVA GAGALANIGD VCVDLRLSGR ALVITGPQTR SVAGDNLAAS 70 80 90 100 110 120 LTDCGFEADV VITRDPRPAE VDRVKSFALD YKADFLIGAG GGRSIDIAKL AAYHLDIPYL 130 140 150 160 170 180 SVPTAASHDG IASAMASLNM DGETKSIPTR APLAIIADTG IISKAPPRLM SAGCGDIISN 190 200 210 220 230 240 YTAILDWRLA KRLKCEDYSE YAAALSSMTA KMVVDMAPSI KPGHEPSAKV VVQALISSGV 250 260 270 280 290 300 AMSIAGSSRP ASGSEHMFAH ALNRIAPGRG LHGELCGIGT IIMMYLHGGD WRMIREALKV 310 320 330 340 350 LGAPASAHEL NIPEDVVVEA LTQAHKIRPE RYTILGNGLT EAAARAAAET TKVI

References

[1]

"Complete sequence of Methanosaeta thermophila PT." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Smith K.S., Ingram-Smith C., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 6194 / PT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000477 Genomic DNA. Translation: ABK14017.1.
RefSeq	YP_842657.1. NC_008553.1.
3D structure databases
ProteinModelPortal	A0B5P3.
ModBase	Search...
Protein-protein interaction databases
STRING	A0B5P3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4461992.
GenomeReviews	Gene locus Mthe_0219 in contig CP000477_GR.
KEGG	mtp:Mthe_0219.
NMPDR	fig|349307.7.peg.226.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	CGVGTIM.
PhylomeDB	A0B5P3.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	MTHE349307:MTHE_0219-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_METTP

Accession

Primary (citable) accession number: A0B5P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	November 28, 2006
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program