P72010 (G1PDH_METTH) 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:	MTH_610

Organism

Methanobacterium thermoautotrophicum (strain Delta H)

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Is also able to catalyze the reverse reaction, i.e. the NAD(P)+-dependent oxidation of G1P but not of G3P. Is not active toward glycerol, dihydroxyacetone, glyceraldehyde-3-phosphate, glyceraldehyde and glycerol-2-phosphate. Ref.4 Ref.7
Catalytic activity	sn-glycerol-1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H. Ref.4
Cofactor	Binds 1 zinc ion per subunit. Ref.6 Ref.7
Enzyme regulation	Partially inhibited by divalent metal cations such as Co2+, Cu2+ and Ni2+. Ref.4
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP MF_00497_A
Subunit structure	Homooctamer. Ref.4
Subcellular location	Cytoplasm Potential HAMAP MF_00497_A.
Miscellaneous	G1PDH is a pro-R type dehydrogenase, which selectively transfers the pro-R hydrogen from NADH to dihydroxyacetonephosphate. HAMAP MF_00497_A
Sequence similarities	Belongs to the glycerol-1-phosphate dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=2.17 mM for DHAP (in the presence of NADH as coenzyme) Ref.4 KM=0.58 mM for DHAP (in the presence of NADPH as coenzyme) KM=0.129 mM for NADH KM=0.025 mM for NADPH KM=16.3 mM for G1P (in the presence of NAD as coenzyme) KM=4.8 mM for G1P (in the presence of NADP as coenzyme) KM=0.127 mM for NAD+ KM=0.270 mM for NADP+ Vmax=610 µmol/min/mg enzyme for DHAP reduction with NADH as coenzyme Vmax=303 µmol/min/mg enzyme for DHAP reduction with NADPH as coenzyme Vmax=39.8 µmol/min/mg enzyme for G1P oxidation with NADH as coenzyme Vmax=23.9 µmol/min/mg enzyme for G1P oxidation with NADPH as coenzyme pH dependence: Optimum pH is 6.6-7-4. Activity decreases gradually at pH over 7.4 or below 6.6. Temperature dependence: Optimum temperature is 75 degrees Celsius.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cytoplasm
Ligand	Metal-binding NAD NADP Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference 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 – 347	347	Glycerol-1-phosphate dehydrogenase [NAD(P)+] HAMAP MF_00497_A		PRO_0000157345
Regions
	Nucleotide binding	94 – 98	5	NAD By similarity
	Nucleotide binding	116 – 119	4	NAD By similarity
Sites
	Metal binding	168	1	Zinc; catalytic Probable
	Metal binding	248	1	Zinc; catalytic Probable
	Metal binding	264	1	Zinc; catalytic Probable
	Binding site	121	1	Substrate Probable
	Binding site	125	1	NAD By similarity
	Binding site	168	1	Substrate Probable
	Binding site	252	1	Substrate Probable

Sequences

	Sequence		Length	Mass (Da)
	P72010 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 46D3600C30515413	FASTA	347	36,963
	10 20 30 40 50 60 MDPRKIQLPR EIYTGPGVIE DTGRICRDLR FEGRAMVVTG PRTLQIAGEA AIESLQAEGF 70 80 90 100 110 120 EVDQVTVDDA TMASVRNVQD GLDGVSVVLG VGGGKVIDVA KMSATLEGLH FISVPTAASH 130 140 150 160 170 180 DGIASPRASI RNGEGTASLE ASSPIGVIAD TEIISRAPFR LLASGCADII SNYTAIMDWK 190 200 210 220 230 240 LAHRLLNERY SESAAALSLM TAKMIIKSAD AIKEGLEESA RLAVKSLISS GIAISIAGSS 250 260 270 280 290 300 RPASGSEHKF SHALDMIAPK PALHGEQCGV GTIMMMHLHG GDWQFIRDAL ARINAPTTAA 310 320 330 340 ELGIDPEYII EALTMAHNIR RERYTILGDR GLTREAAERL AKITEVI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent." Koga Y., Kyuragi T., Nishihara M., Sone N. J. Mol. Evol. 46:54-63(1998) [PubMed: 9419225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Delta H.
[2]	Erratum Koga Y., Kyuragi T., Nishihara M., Sone N. J. Mol. Evol. 47:631-631(1998) [PubMed: 9797414] [Abstract]
[3]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.
[4]	"Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of Archaea." Nishihara M., Koga Y. J. Biochem. 122:572-576(1997) [PubMed: 9348086] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-23, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES. Strain: Delta H.
[5]	Erratum Nishihara M., Koga Y. J. Biochem. 123:194-194(1998)
[6]	"Analysis of membrane stereochemistry with homology modeling of sn-glycerol-1-phosphate dehydrogenase." Daiyasu H., Hiroike T., Koga Y., Toh H. Protein Eng. 15:987-995(2002) [PubMed: 12601138] [Abstract] Cited for: COFACTOR, 3D-STRUCTURE MODELING.
[7]	"Transfer of pro-R hydrogen from NADH to dihydroxyacetonephosphate by sn-glycerol-1-phosphate dehydrogenase from the archaeon Methanothermobacter thermautotrophicus." Koga Y., Sone N., Noguchi S., Morii H. Biosci. Biotechnol. Biochem. 67:1605-1608(2003) [PubMed: 12913312] [Abstract] Cited for: FUNCTION, COFACTOR, STEREOSPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D88555 Genomic DNA. Translation: BAA13644.1. AE000666 Genomic DNA. Translation: AAB85116.1.
PIR	B69181.
RefSeq	NP_275753.1. NC_000916.1.
3D structure databases
ProteinModelPortal	P72010.
ModBase	Search...
Protein-protein interaction databases
STRING	P72010.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1470571.
GenomeReviews	Gene locus MTH_610 in contig AE000666_GR.
KEGG	mth:MTH610.
NMPDR	fig|187420.1.peg.608.
Phylogenomic databases
eggNOG	arNOG04488.
HOGENOM	HBG672951.
OMA	CGVGTIM.
ProtClustDB	PRK00843.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14507. MTHE187420:MTH610-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_METTH

Accession

Primary (citable) accession number: P72010

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	February 1, 1997
Last modified:	November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program