Reviewed, UniProtKB/Swiss-Prot A3CX71 (G1PDH_METMJ)

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:	Memar_2045

Organism

Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]

Taxonomic identifier

368407 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanomicrobiales › Methanomicrobiaceae › Methanoculleus

Protein attributes

Sequence length	360 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 – 360	360	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497		PRO_0000350656
Regions
	Nucleotide binding	108 – 112	5	NAD By similarity
	Nucleotide binding	130 – 133	4	NAD By similarity
Sites
	Metal binding	182	1	Zinc; catalytic By similarity
	Metal binding	262	1	Zinc; catalytic By similarity
	Metal binding	278	1	Zinc; catalytic By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	139	1	NAD By similarity
	Binding site	182	1	Substrate By similarity
	Binding site	266	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3CX71-1 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 2059C055CB437EC6	FASTA	360	38,029
	10 20 30 40 50 60 MSADRINLLR TKVFDKSKWM QLPRDVVIGH DVIEQIPAVC EDLALGDSVL IVSGGQTRDI 70 80 90 100 110 120 AGKRVEALLA GSYDVVTFAA NDGNPFETIR KAEEAAATAG FVIGVGGGRV IDTAKIASYN 130 140 150 160 170 180 TDRHFISVPT AASHDGIASS RASVPTADGN VSLAAEPPIA VVADTAVIAS APHRLLASGC 190 200 210 220 230 240 ADIIANYTAI LDWELSHRLR GEPLSEYALT LSRMTAEILF KNADLIKPHS EESAWLVTKA 250 260 270 280 290 300 LVSSGVAMSI AGSSRPGSGG EHKFSHALEK LAPGKGLHGE KCGIGAIITM YLHGGDWEGI 310 320 330 340 350 360 RDSLKKIGAP TTPAAIGVDD ETAVAALLAA RTIRPERFTI LDMGLTEESA RDLVKMLYRE

References

[1]

"Complete sequence of Methanoculleus marisnigri JR1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Anderson I., Sieprawska-Lupa M., Whitman W., Woese C., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000562 Genomic DNA. Translation: ABN57971.1.
RefSeq	YP_001047953.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A3CX71.
Genome annotation databases
GeneID	4847602.
GenomeReviews	Gene locus Memar_2045 in contig CP000562_GR.
KEGG	mem:Memar_2045.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	SESSAIF.
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_METMJ

Accession

Primary (citable) accession number: A3CX71

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	March 20, 2007
Last modified:	November 3, 2009
This is version 20 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)