Reviewed, UniProtKB/Swiss-Prot Q8PZA4 (G1PDH_METMA)

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):
    sn-glycerol-1-phosphate dehydrogenase
    Enantiomeric glycerophosphate synthase

Gene names

Name:	egsA
Ordered Locus Names:	MM_0590

Organism

Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]

Taxonomic identifier

2209 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. HAMAP MF_00497
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497
Subcellular location	Cytoplasm Potential.
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	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW phospholipid biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-dehydroquinate synthase activity Inferred from electronic annotation. Source: InterPro glycerol-1-phosphate dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: HAMAP zinc 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 – 356	356	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000157344
Regions
	Nucleotide binding	103 – 107	5	NAD By similarity
	Nucleotide binding	125 – 128	4	NAD By similarity
Sites
	Metal binding	177	1	Zinc; catalytic By similarity
	Metal binding	257	1	Zinc; catalytic By similarity
	Metal binding	273	1	Zinc; catalytic By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	134	1	NAD By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	261	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PZA4-1 [UniParc]. Last modified October 10, 2002. Version 1. Checksum: 4AC98A82E6AC2F31	FASTA	356	38,065
	10 20 30 40 50 60 MKLTINKNSA KWMQLPRDVL VGHGVLEEVG DVCRDLKLKG NALIVTGSTT QDVAGKRVSR 70 80 90 100 110 120 LLEDAGNSTE TVLTCRATME EVDKLMEKAL NTEATFLLGV GSGRSIDLAK LASTRLEIPF 130 140 150 160 170 180 ISVPTAASHD GIASSRASVI DNGKNASIQA QAPLAVIADT EIISAAPYRF LAAGCGDIIS 190 200 210 220 230 240 NYTAVLDWEL ASRLRNEYFG EYAAALSRMA ARVVIENADS IKPDHETSAR LVVKALVSNG 250 260 270 280 290 300 VAMSIAGSSR PASGSEHMFS HALDRIAPKA ALHGEQCGVG TIMMMYLHGG NWQEIRDALK 310 320 330 340 350 KIGAPTNAEE LGIEDKYIIE ALLQAHSIRP DRYTILGNGL TLSAAEKVAR ITKVIN

References

[1]

"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G. J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008384 Genomic DNA. Translation: AAM30286.1.
RefSeq	NP_632614.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1478932.
GenomeReviews	Gene locus MM_0590 in contig AE008384_GR.
KEGG	mma:MM_0590.
NMPDR	fig|192952.1.peg.590.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8PZA4.
OMA	YTAVLDW.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM0590-MON.
BRENDA	1.1.1.261. 261165.
Family and domain databases
HAMAP	MF_00497. [Tree]
InterPro	IPR002658. DHQ_synth_AroB. IPR016205. Glycerol_DH. [Graphical view]
Pfam	PF01761. DHQ_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000112. Glycerol_dehydrogenase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

G1PDH_METMA

Accession

Primary (citable) accession number: Q8PZA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)