Reviewed, UniProtKB/Swiss-Prot Q8TJU1 (G1PDH_METAC)

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
Synonyms:	gldA
Ordered Locus Names:	MA_3686

Organism

Methanosarcina acetivorans [Complete proteome] [HAMAP]

Taxonomic identifier

2214 [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_0000157341
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)
	Q8TJU1-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: A2229E455BBFEA2F	FASTA	356	38,029
	10 20 30 40 50 60 MKLTINKNSA KWMQLPRDVL VGHGVLEEIG DVCRDLKLKG NALIVTGNTT RDVAGKRVST 70 80 90 100 110 120 LLENAGSSTE MVLTCRATME EVDKIMQKAS ETGATFLLGI GSGRSIDLAK LASTRLEIPF 130 140 150 160 170 180 ISVPTAASHD GIASSRASII DNGKNASVQA QAPIAVVADT EIISAAPFRF LVAGCGDIIS 190 200 210 220 230 240 NYTAVLDWEL ASRLRNEYFG EYAAALSRMA ARVVIENADS IKPEHETSAR LVVKALVSNG 250 260 270 280 290 300 VAMSIAGSSR PASGSEHMFS HALDRIAPKP ALHGEQCGVG TIMMMYLHGG NWQEIRDALK 310 320 330 340 350 KIGAPTNAEE LGIEDRYIVE ALLHAHSIRP DRYTILGNGL TPSAAEKVAR ITKVIS

References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE010299 Genomic DNA. Translation: AAM07041.1.
RefSeq	NP_618561.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1475579.
GenomeReviews	Gene locus MA_3686 in contig AE010299_GR.
KEGG	mac:MA3686.
NMPDR	fig|188937.1.peg.3587.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8TJU1.
OMA	YTAVLDW.
Enzyme and pathway databases
BioCyc	MACE188937:MA3686-MON.
BRENDA	1.1.1.261. 275708.
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_METAC

Accession

Primary (citable) accession number: Q8TJU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 52 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)