Q2NFL8 (G1PDH_METST) 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:	Msp_0997

Organism

Methanosphaera stadtmanae (strain DSM 3091) [Complete proteome] [HAMAP]

Taxonomic identifier

339860 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanosphaera

Protein attributes

Sequence length	348 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	Homooctamer 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 – 348	348	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_1000050604
Regions
	Nucleotide binding	94 – 98	5	NAD By similarity
Sites
	Metal binding	168	1	Zinc; catalytic By similarity
	Metal binding	248	1	Zinc; catalytic By similarity
	Metal binding	264	1	Zinc; catalytic By similarity
	Binding site	116	1	NAD By similarity
	Binding site	121	1	Substrate By similarity
	Binding site	125	1	NAD By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	252	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2NFL8 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: AC463A1913443B19	FASTA	348	37,276
	10 20 30 40 50 60 MDFRNVQLPR EIHSGSGIIE EIGDVCDNLL PKKDVTILTG PTTKKIAGNH VIEILKESNY 70 80 90 100 110 120 EISEITVNLA TEESVEEVVK DSKDSSAILG VGGGKVIDVA KMASTINHIP LISVPTTAAH 130 140 150 160 170 180 DGMASPRASI KNDKGTVSLK ANAPFALIAD TTIISQAPYR FTAAGFSDII SNLTAVEDWK 190 200 210 220 230 240 LAYKLINEPF SDSAAALSVM TAKLLIDEAD NIHPNNENSA SVVVKGLISS GMAISIAGNS 250 260 270 280 290 300 RPASGSEHKF SHALDMIAPK PALHGEQCGV GTIMMMYLQG GDWQNIKSVL EKVNAPTTAK 310 320 330 340 ELGIDEEYII EALIQAHNIR KERYTILGDR GLTREAAENI ALKTHVIE

References

[1]

"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis." Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K. J. Bacteriol. 188:642-658(2006) [PubMed: 16385054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 3091.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000102 Genomic DNA. Translation: ABC57385.1.
RefSeq	YP_448028.1. NC_007681.1.
3D structure databases
ProteinModelPortal	Q2NFL8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2NFL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3855278.
GenomeReviews	Gene locus Msp_0997 in contig CP000102_GR.
KEGG	mst:Msp_0997.
NMPDR	fig|339860.6.peg.956.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	CGVGTIM.
PhylomeDB	Q2NFL8.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	MSTA339860:MSP_0997-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_METST

Accession

Primary (citable) accession number: Q2NFL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 7, 2006
Last modified:	November 16, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program