ID G1PDH_BACSU Reviewed; 394 AA.
AC P94527; O05092;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+];
DE Short=G1P dehydrogenase;
DE Short=G1PDH;
DE EC=1.1.1.261 {ECO:0000269|PubMed:18558723};
DE AltName: Full=Arabinose operon protein AraM;
DE AltName: Full=Enantiomeric glycerophosphate synthase;
DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase;
GN Name=egsA; Synonyms=araM, yseB; OrderedLocusNames=BSU28760;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9084180; DOI=10.1099/00221287-143-3-957;
RA Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.;
RT "The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence,
RT genetic organization and expression.";
RL Microbiology 143:957-969(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP TRANSCRIPTIONAL REGULATION.
RX PubMed=10417639; DOI=10.1046/j.1365-2958.1999.01484.x;
RA Mota L.J., Tavares P., Sa-Nogueira I.M.G.;
RT "Mode of action of AraR, the key regulator of L-arabinose metabolism in
RT Bacillus subtilis.";
RL Mol. Microbiol. 33:476-489(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=18558723; DOI=10.1021/bi8005779;
RA Guldan H., Sterner R., Babinger P.;
RT "Identification and characterization of a bacterial glycerol-1-phosphate
RT dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis.";
RL Biochemistry 47:7376-7384(2008).
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 probably used for the
CC synthesis of phosphoglycerolipids in Gram-positive bacterial species.
CC Prefers NADH over NADPH as coenzyme. Is also able to catalyze the
CC reverse reaction, i.e. the NAD(+)-dependent oxidation of G1P but not of
CC G3P. Does not possess glycerol dehydrogenase activity.
CC {ECO:0000269|PubMed:18558723}.
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:18558723};
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:18558723};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:18558723};
CC Note=Binds 1 nickel ion per subunit. Is not active with other divalent
CC metal cations such as Zn(2+), Cu(2+), Ca(2+), Mg(2+), Mn(2+) or Fe(2+).
CC {ECO:0000269|PubMed:18558723};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 uM for DHAP {ECO:0000269|PubMed:18558723};
CC KM=16.0 uM for NADH {ECO:0000269|PubMed:18558723};
CC KM=1370 uM for G1P {ECO:0000269|PubMed:18558723};
CC KM=59.3 uM for NAD(+) {ECO:0000269|PubMed:18558723};
CC pH dependence:
CC Optimum pH is 8.2. {ECO:0000269|PubMed:18558723};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18558723}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Transcription is repressed by glucose and by the binding of
CC AraR to the operon promoter. L-arabinose acts as an inducer by
CC inhibiting the binding of AraR to the DNA, thus allowing expression of
CC the gene. {ECO:0000269|PubMed:10417639}.
CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X89810; CAA61933.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99591.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14836.1; -; Genomic_DNA.
DR PIR; H69587; H69587.
DR RefSeq; NP_390754.1; NC_000964.3.
DR RefSeq; WP_003229504.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P94527; -.
DR SMR; P94527; -.
DR STRING; 224308.BSU28760; -.
DR SwissLipids; SLP:000001803; -.
DR PaxDb; 224308-BSU28760; -.
DR EnsemblBacteria; CAB14836; CAB14836; BSU_28760.
DR GeneID; 938011; -.
DR KEGG; bsu:BSU28760; -.
DR PATRIC; fig|224308.179.peg.3124; -.
DR eggNOG; COG0371; Bacteria.
DR InParanoid; P94527; -.
DR OrthoDB; 9763580at2; -.
DR PhylomeDB; P94527; -.
DR BioCyc; BSUB:BSU28760-MONOMER; -.
DR SABIO-RK; P94527; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IBA:GO_Central.
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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd08175; G1PDH; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR HAMAP; MF_00497_B; G1P_dehydrogenase_B; 1.
DR InterPro; IPR023003; G1P_dehydrogenase_bac.
DR InterPro; IPR032837; G1PDH.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13685; Fe-ADH_2; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Metal-binding; NAD; NADP;
KW Nickel; Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome.
FT CHAIN 1..394
FT /note="Glycerol-1-phosphate dehydrogenase [NAD(P)+]"
FT /id="PRO_0000064659"
FT BINDING 54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 116..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138..141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 350
FT /note="Y -> D (in Ref. 1; CAA61933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 43057 MW; 3F5F5230917B20DD CRC64;
MNRIAADVQR AFENAGEKTL PIKVEEIVLG KQAADSLLDY VKRKNNQHIV LVCDANTHRI
AGIDLENRLN QEGFQAECLI IPENEAGDVT ADERSLIHVL IHTKQPTDVM IAVGSGTIHD
IVRFAAFQRD LPFISYPTAP SVDGFTSAGA PIILYGTKTT IQTKAPSALF ADLDLLKAAP
QSMVAAGFGD MLGKITSLAD WEISRHLAGE PYSPAGAKIV QEALAACIEH TEDIAMKTET
GIRVLMESLL VSGLVMLALD HSRPASGGEH HISHWIEMEL MEKKRPQILH GAKVGCAAVL
LTDTYRKLAQ DDGLNEFSPS RREAIQSAYQ TLPRGEVLAD WLRSAGGPAY FDEIGVGQDS
VKNAFRHAHT LRDRCTGLRI INENKTLINH GLYE
//
