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Glycerol-3-phosphate dehydrogenase [NAD(P) ] (EC 1.1.1.94) (NAD(P)H-dependent dihydroxyacetone-phosphate reductase) (NAD(P)H-dependent glycerol-3-phosphate dehydrogenase)

 GPDA_BACSU              Reviewed;         345 AA.
P46919;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
29-AUG-2003, sequence version 2.
12-SEP-2018, entry version 138.
RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00394};
EC=1.1.1.94 {ECO:0000255|HAMAP-Rule:MF_00394};
AltName: Full=NAD(P)H-dependent dihydroxyacetone-phosphate reductase;
AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00394};
Name=gpsA {ECO:0000255|HAMAP-Rule:MF_00394}; Synonyms=glyC;
OrderedLocusNames=BSU22830;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
ACTIVITY REGULATION.
STRAIN=168;
PubMed=7592341; DOI=10.1128/jb.177.20.5899-5905.1995;
Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.;
"Synthesis of sn-glycerol 3-phosphate, a key precursor of membrane
lipids, in Bacillus subtilis.";
J. Bacteriol. 177:5899-5905(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
Serror P.;
"Sequence analysis of the Bacillus subtilis chromosome region between
the serA and kdg loci cloned in a yeast artificial chromosome.";
Microbiology 142:2005-2016(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
SUBCELLULAR LOCATION.
PubMed=15743965; DOI=10.1128/JB.187.6.2163-2174.2005;
Nishibori A., Kusaka J., Hara H., Umeda M., Matsumoto K.;
"Phosphatidylethanolamine domains and localization of phospholipid
synthases in Bacillus subtilis membranes.";
J. Bacteriol. 187:2163-2174(2005).
-!- FUNCTION: Involved in the biosynthesis of the sn-glycerol 3-
phosphate required for phospholipid synthesis.
{ECO:0000269|PubMed:7592341}.
-!- CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + NAD(P)(+) =
glycerone phosphate + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_00394}.
-!- ACTIVITY REGULATION: Slightly inhibited by sn-glycerol 3-
phosphate. {ECO:0000269|PubMed:7592341}.
-!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
metabolism. {ECO:0000255|HAMAP-Rule:MF_00394}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394,
ECO:0000269|PubMed:15743965}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are auxotrophic for
glycerol. {ECO:0000269|PubMed:7592341}.
-!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00394}.
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EMBL; U32164; AAA86746.1; -; Genomic_DNA.
EMBL; L47648; AAC83967.1; -; Genomic_DNA.
EMBL; AL009126; CAB14199.1; -; Genomic_DNA.
PIR; H69636; H69636.
RefSeq; NP_390164.1; NC_000964.3.
RefSeq; WP_003230566.1; NZ_JNCM01000036.1.
ProteinModelPortal; P46919; -.
SMR; P46919; -.
STRING; 224308.Bsubs1_010100012541; -.
PaxDb; P46919; -.
PRIDE; P46919; -.
EnsemblBacteria; CAB14199; CAB14199; BSU22830.
GeneID; 938989; -.
KEGG; bsu:BSU22830; -.
PATRIC; fig|224308.179.peg.2488; -.
eggNOG; ENOG4105CSF; Bacteria.
eggNOG; COG0240; LUCA.
HOGENOM; HOG000246854; -.
InParanoid; P46919; -.
KO; K00057; -.
OMA; WLCKGFE; -.
PhylomeDB; P46919; -.
BioCyc; BSUB:BSU22830-MONOMER; -.
UniPathway; UPA00940; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IDA:UniProtKB.
GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 1.10.1040.10; -; 1.
HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 1.
InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
InterPro; IPR013328; 6PGD_dom2.
InterPro; IPR006168; G3P_DH_NAD-dep.
InterPro; IPR006109; G3P_DH_NAD-dep_C.
InterPro; IPR011128; G3P_DH_NAD-dep_N.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF07479; NAD_Gly3P_dh_C; 1.
Pfam; PF01210; NAD_Gly3P_dh_N; 1.
PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
PRINTS; PR00077; GPDHDRGNASE.
SUPFAM; SSF48179; SSF48179; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00957; NAD_G3PDH; 1.
3: Inferred from homology;
Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
NAD; Oxidoreductase; Phospholipid biosynthesis;
Phospholipid metabolism; Reference proteome.
CHAIN 1 345 Glycerol-3-phosphate dehydrogenase
[NAD(P)+].
/FTId=PRO_0000137926.
NP_BIND 8 13 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
REGION 256 257 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00394}.
ACT_SITE 192 192 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00394}.
BINDING 106 106 NAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00394}.
BINDING 106 106 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00394}.
BINDING 141 141 NAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00394}.
BINDING 256 256 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
BINDING 282 282 NAD. {ECO:0000255|HAMAP-Rule:MF_00394}.
CONFLICT 130 130 K -> R (in Ref. 1; AAA86746).
{ECO:0000305}.
CONFLICT 149 149 P -> A (in Ref. 1; AAA86746).
{ECO:0000305}.
SEQUENCE 345 AA; 37436 MW; E17CD83A909C1096 CRC64;
MKKVTMLGAG SWGTALALVL TDNGNEVCVW AHRADLIHQI NELHENKDYL PNVKLSTSIK
GTTDMKEAVS DADVIIVAVP TKAIREVLRQ AVPFITKKAV FVHVSKGIEP DSLLRISEIM
EIELPSDVRK DIVVLSGPSH AEEVGLRHPT TVTASSKSMR AAEEVQDLFI NHNFRVYTNP
DIIGVEIGGA LKNIIALAAG ITDGLGYGDN AKAALITRGL AEIARLGTKM GGNPLTFSGL
TGVGDLIVTC TSVHSRNWRA GNLLGKGYKL EDVLEEMGMV VEGVRTTKAA YQLSKKYDVK
MPITEALHQV LFNGQKVETA VESLMARGKT HEMEDLVNTF ENQVK


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