G1PDH_METTH
ID G1PDH_METTH Reviewed; 347 AA.
AC P72010;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+];
DE Short=G1P dehydrogenase;
DE Short=G1PDH;
DE EC=1.1.1.261;
DE AltName: Full=Enantiomeric glycerophosphate synthase;
DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase;
GN Name=egsA; OrderedLocusNames=MTH_610;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9419225; DOI=10.1007/pl00006283;
RA Koga Y., Kyuragi T., Nishihara M., Sone N.;
RT "Did archaeal and bacterial cells arise independently from noncellular
RT precursors? A hypothesis stating that the advent of membrane phospholipid
RT with enantiomeric glycerophosphate backbones caused the separation of the
RT two lines of descent.";
RL J. Mol. Evol. 46:54-63(1998).
RN [2]
RP ERRATUM OF PUBMED:9419225.
RX PubMed=9797414; DOI=10.1007/pl00006419;
RA Koga Y., Kyuragi T., Nishihara M., Sone N.;
RL J. Mol. Evol. 47:631-631(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [4]
RP PROTEIN SEQUENCE OF 1-23, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9348086; DOI=10.1093/oxfordjournals.jbchem.a021791;
RA Nishihara M., Koga Y.;
RT "Purification and properties of sn-glycerol-1-phosphate dehydrogenase from
RT Methanobacterium thermoautotrophicum: characterization of the biosynthetic
RT enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids
RT of Archaea.";
RL J. Biochem. 122:572-576(1997).
RN [5]
RP ERRATUM OF PUBMED:9348086.
RA Nishihara M., Koga Y.;
RL J. Biochem. 123:194-194(1998).
RN [6]
RP COFACTOR, AND 3D-STRUCTURE MODELING.
RX PubMed=12601138; DOI=10.1093/protein/15.12.987;
RA Daiyasu H., Hiroike T., Koga Y., Toh H.;
RT "Analysis of membrane stereochemistry with homology modeling of sn-
RT glycerol-1-phosphate dehydrogenase.";
RL Protein Eng. 15:987-995(2002).
RN [7]
RP FUNCTION, COFACTOR, AND STEREOSPECIFICITY.
RX PubMed=12913312; DOI=10.1271/bbb.67.1605;
RA Koga Y., Sone N., Noguchi S., Morii H.;
RT "Transfer of pro-R hydrogen from NADH to dihydroxyacetonephosphate by sn-
RT glycerol-1-phosphate dehydrogenase from the archaeon Methanothermobacter
RT thermautotrophicus.";
RL Biosci. Biotechnol. Biochem. 67:1605-1608(2003).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of
CC dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-
CC phosphate (G1P). The G1P thus generated is used as the glycerophosphate
CC backbone of phospholipids in the cellular membranes of Archaea. Is also
CC able to catalyze the reverse reaction, i.e. the NAD(P)(+)-dependent
CC oxidation of G1P but not of G3P. Is not active toward glycerol,
CC dihydroxyacetone, glyceraldehyde-3-phosphate, glyceraldehyde and
CC glycerol-2-phosphate. {ECO:0000269|PubMed:12913312,
CC ECO:0000269|PubMed:9348086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:21412, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57642, ChEBI:CHEBI:57685,
CC ChEBI:CHEBI:57945; EC=1.1.1.261;
CC Evidence={ECO:0000269|PubMed:9348086};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + sn-glycerol 1-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADPH; Xref=Rhea:RHEA:21416, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57685, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.261;
CC Evidence={ECO:0000269|PubMed:9348086};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12601138, ECO:0000269|PubMed:12913312};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12601138,
CC ECO:0000269|PubMed:12913312};
CC -!- ACTIVITY REGULATION: Partially inhibited by divalent metal cations such
CC as Co(2+), Cu(2+) and Ni(2+). {ECO:0000269|PubMed:9348086}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.17 mM for DHAP (in the presence of NADH as coenzyme)
CC {ECO:0000269|PubMed:9348086};
CC KM=0.58 mM for DHAP (in the presence of NADPH as coenzyme)
CC {ECO:0000269|PubMed:9348086};
CC KM=0.129 mM for NADH {ECO:0000269|PubMed:9348086};
CC KM=0.025 mM for NADPH {ECO:0000269|PubMed:9348086};
CC KM=16.3 mM for G1P (in the presence of NAD as coenzyme)
CC {ECO:0000269|PubMed:9348086};
CC KM=4.8 mM for G1P (in the presence of NADP as coenzyme)
CC {ECO:0000269|PubMed:9348086};
CC KM=0.127 mM for NAD(+) {ECO:0000269|PubMed:9348086};
CC KM=0.270 mM for NADP(+) {ECO:0000269|PubMed:9348086};
CC Vmax=610 umol/min/mg enzyme for DHAP reduction with NADH as coenzyme
CC {ECO:0000269|PubMed:9348086};
CC Vmax=303 umol/min/mg enzyme for DHAP reduction with NADPH as coenzyme
CC {ECO:0000269|PubMed:9348086};
CC Vmax=39.8 umol/min/mg enzyme for G1P oxidation with NADH as coenzyme
CC {ECO:0000269|PubMed:9348086};
CC Vmax=23.9 umol/min/mg enzyme for G1P oxidation with NADPH as coenzyme
CC {ECO:0000269|PubMed:9348086};
CC pH dependence:
CC Optimum pH is 6.6-7-4. Activity decreases gradually at pH over 7.4 or
CC below 6.6. {ECO:0000269|PubMed:9348086};
CC Temperature dependence:
CC Optimum temperature is 75 degrees Celsius.
CC {ECO:0000269|PubMed:9348086};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:9348086}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: G1PDH is a pro-R type dehydrogenase, which selectively
CC transfers the pro-R hydrogen from NADH to dihydroxyacetonephosphate.
CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D88555; BAA13644.1; -; Genomic_DNA.
DR EMBL; AE000666; AAB85116.1; -; Genomic_DNA.
DR PIR; B69181; B69181.
DR RefSeq; WP_010876249.1; NC_000916.1.
DR AlphaFoldDB; P72010; -.
DR SMR; P72010; -.
DR STRING; 187420.MTH_610; -.
DR EnsemblBacteria; AAB85116; AAB85116; MTH_610.
DR GeneID; 1470571; -.
DR KEGG; mth:MTH_610; -.
DR PATRIC; fig|187420.15.peg.591; -.
DR HOGENOM; CLU_038362_0_0_2; -.
DR OMA; ALHGEQC; -.
DR BioCyc; MetaCyc:MON-14507; -.
DR SABIO-RK; P72010; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106357; F:glycerol-1-phosphate dehydrogenase [NAD+] activity; IEA:RHEA.
DR GO; GO:0106358; F:glycerol-1-phosphate dehydrogenase [NADP+] activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1.
DR InterPro; IPR023002; G1P_dehydrogenase_arc.
DR InterPro; IPR032837; G1PDH.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; PTHR43616; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; NAD; NADP; Oxidoreductase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Zinc.
FT CHAIN 1..347
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000157345"
FT BINDING 94..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 36963 MW; 46D3600C30515413 CRC64;
MDPRKIQLPR EIYTGPGVIE DTGRICRDLR FEGRAMVVTG PRTLQIAGEA AIESLQAEGF
EVDQVTVDDA TMASVRNVQD GLDGVSVVLG VGGGKVIDVA KMSATLEGLH FISVPTAASH
DGIASPRASI RNGEGTASLE ASSPIGVIAD TEIISRAPFR LLASGCADII SNYTAIMDWK
LAHRLLNERY SESAAALSLM TAKMIIKSAD AIKEGLEESA RLAVKSLISS GIAISIAGSS
RPASGSEHKF SHALDMIAPK PALHGEQCGV GTIMMMHLHG GDWQFIRDAL ARINAPTTAA
ELGIDPEYII EALTMAHNIR RERYTILGDR GLTREAAERL AKITEVI
