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Glycerol-1-phosphate dehydrogenase [NAD(P) ] (G1P dehydrogenase) (G1PDH) (EC 1.1.1.261) (Enantiomeric glycerophosphate synthase) (sn-glycerol-1-phosphate dehydrogenase)

 G1PDH_METTH             Reviewed;         347 AA.
P72010;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-FEB-2018, entry version 118.
RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+];
Short=G1P dehydrogenase;
Short=G1PDH;
EC=1.1.1.261;
AltName: Full=Enantiomeric glycerophosphate synthase;
AltName: Full=sn-glycerol-1-phosphate dehydrogenase;
Name=egsA; OrderedLocusNames=MTH_610;
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /
JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
thermoautotrophicum).
Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
Methanobacteriaceae; Methanothermobacter.
NCBI_TaxID=187420;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
PubMed=9419225; DOI=10.1007/PL00006283;
Koga Y., Kyuragi T., Nishihara M., Sone N.;
"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.";
J. Mol. Evol. 46:54-63(1998).
[2]
ERRATUM.
PubMed=9797414; DOI=10.1007/PL00006419;
Koga Y., Kyuragi T., Nishihara M., Sone N.;
J. Mol. Evol. 47:631-631(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
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.;
"Complete genome sequence of Methanobacterium thermoautotrophicum
deltaH: functional analysis and comparative genomics.";
J. Bacteriol. 179:7135-7155(1997).
[4]
PROTEIN SEQUENCE OF 1-23, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
SPECIFICITY, ENZYME REGULATION, SUBUNIT, AND BIOPHYSICOCHEMICAL
PROPERTIES.
STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
PubMed=9348086; DOI=10.1093/oxfordjournals.jbchem.a021791;
Nishihara M., Koga Y.;
"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.";
J. Biochem. 122:572-576(1997).
[5]
ERRATUM.
Nishihara M., Koga Y.;
J. Biochem. 123:194-194(1998).
[6]
COFACTOR, AND 3D-STRUCTURE MODELING.
PubMed=12601138; DOI=10.1093/protein/15.12.987;
Daiyasu H., Hiroike T., Koga Y., Toh H.;
"Analysis of membrane stereochemistry with homology modeling of sn-
glycerol-1-phosphate dehydrogenase.";
Protein Eng. 15:987-995(2002).
[7]
FUNCTION, COFACTOR, AND STEREOSPECIFICITY.
PubMed=12913312; DOI=10.1271/bbb.67.1605;
Koga Y., Sone N., Noguchi S., Morii H.;
"Transfer of pro-R hydrogen from NADH to dihydroxyacetonephosphate by
sn-glycerol-1-phosphate dehydrogenase from the archaeon
Methanothermobacter thermautotrophicus.";
Biosci. Biotechnol. Biochem. 67:1605-1608(2003).
-!- 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. {ECO:0000269|PubMed:12913312,
ECO:0000269|PubMed:9348086}.
-!- CATALYTIC ACTIVITY: sn-glycerol 1-phosphate + NAD(P)(+) =
glycerone phosphate + NAD(P)H. {ECO:0000269|PubMed:9348086}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:12601138,
ECO:0000269|PubMed:12913312};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12601138,
ECO:0000269|PubMed:12913312};
-!- ENZYME REGULATION: Partially inhibited by divalent metal cations
such as Co(2+), Cu(2+) and Ni(2+). {ECO:0000269|PubMed:9348086}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.17 mM for DHAP (in the presence of NADH as coenzyme)
{ECO:0000269|PubMed:9348086};
KM=0.58 mM for DHAP (in the presence of NADPH as coenzyme)
{ECO:0000269|PubMed:9348086};
KM=0.129 mM for NADH {ECO:0000269|PubMed:9348086};
KM=0.025 mM for NADPH {ECO:0000269|PubMed:9348086};
KM=16.3 mM for G1P (in the presence of NAD as coenzyme)
{ECO:0000269|PubMed:9348086};
KM=4.8 mM for G1P (in the presence of NADP as coenzyme)
{ECO:0000269|PubMed:9348086};
KM=0.127 mM for NAD(+) {ECO:0000269|PubMed:9348086};
KM=0.270 mM for NADP(+) {ECO:0000269|PubMed:9348086};
Vmax=610 umol/min/mg enzyme for DHAP reduction with NADH as
coenzyme {ECO:0000269|PubMed:9348086};
Vmax=303 umol/min/mg enzyme for DHAP reduction with NADPH as
coenzyme {ECO:0000269|PubMed:9348086};
Vmax=39.8 umol/min/mg enzyme for G1P oxidation with NADH as
coenzyme {ECO:0000269|PubMed:9348086};
Vmax=23.9 umol/min/mg enzyme for G1P oxidation with NADPH as
coenzyme {ECO:0000269|PubMed:9348086};
pH dependence:
Optimum pH is 6.6-7-4. Activity decreases gradually at pH over
7.4 or below 6.6. {ECO:0000269|PubMed:9348086};
Temperature dependence:
Optimum temperature is 75 degrees Celsius.
{ECO:0000269|PubMed:9348086};
-!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
metabolism.
-!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:9348086}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- MISCELLANEOUS: G1PDH is a pro-R type dehydrogenase, which
selectively transfers the pro-R hydrogen from NADH to
dihydroxyacetonephosphate.
-!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase
family. {ECO:0000305}.
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EMBL; D88555; BAA13644.1; -; Genomic_DNA.
EMBL; AE000666; AAB85116.1; -; Genomic_DNA.
PIR; B69181; B69181.
RefSeq; WP_010876249.1; NC_000916.1.
ProteinModelPortal; P72010; -.
SMR; P72010; -.
STRING; 187420.MTH610; -.
EnsemblBacteria; AAB85116; AAB85116; MTH_610.
GeneID; 1470571; -.
KEGG; mth:MTH_610; -.
PATRIC; fig|187420.15.peg.591; -.
eggNOG; arCOG00982; Archaea.
eggNOG; COG0371; LUCA.
HOGENOM; HOG000295683; -.
KO; K00096; -.
OMA; WYEASVS; -.
OrthoDB; POG093Z05WV; -.
BioCyc; MetaCyc:MONOMER-14507; -.
BioCyc; MTHE187420:G1G16-575-MONOMER; -.
SABIO-RK; P72010; -.
UniPathway; UPA00940; -.
Proteomes; UP000005223; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050492; F:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
CDD; cd08173; Gro1PDH; 1.
HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1.
InterPro; IPR023002; G1P_dehydrogenase_arc.
InterPro; IPR032837; G1PDH.
InterPro; IPR016205; Glycerol_DH.
PANTHER; PTHR43616; PTHR43616; 1.
Pfam; PF13685; Fe-ADH_2; 1.
PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Lipid biosynthesis; Lipid metabolism; Metal-binding; NAD; NADP;
Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
Reference proteome; Zinc.
CHAIN 1 347 Glycerol-1-phosphate dehydrogenase
[NAD(P)+].
/FTId=PRO_0000157345.
NP_BIND 94 98 NAD. {ECO:0000250}.
NP_BIND 116 119 NAD. {ECO:0000250}.
METAL 168 168 Zinc; catalytic. {ECO:0000305}.
METAL 248 248 Zinc; catalytic. {ECO:0000305}.
METAL 264 264 Zinc; catalytic. {ECO:0000305}.
BINDING 121 121 Substrate. {ECO:0000305}.
BINDING 125 125 NAD. {ECO:0000250}.
BINDING 168 168 Substrate. {ECO:0000305}.
BINDING 252 252 Substrate. {ECO:0000305}.
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


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