ID   GLPD_BACSU              Reviewed;         555 AA.
AC   P18158;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Aerobic glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=BSU09300;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2127799; DOI=10.1099/00221287-136-12-2367;
RA   Holmberg C., Beijer L., Rutberg B., Rutberg L.;
RT   "Glycerol catabolism in Bacillus subtilis: nucleotide sequence of the genes
RT   encoding glycerol kinase (glpK) and glycerol-3-phosphate dehydrogenase
RT   (glpD).";
RL   J. Gen. Microbiol. 136:2367-2375(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
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   SEQUENCE REVISION TO 385-386.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   TRANSCRIPTIONAL REGULATION.
RX   PubMed=1809833; DOI=10.1111/j.1365-2958.1991.tb01849.x;
RA   Holmberg C., Rutberg B.;
RT   "Expression of the gene encoding glycerol-3-phosphate dehydrogenase (glpD)
RT   in Bacillus subtilis is controlled by antitermination.";
RL   Mol. Microbiol. 5:2891-2900(1991).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC       route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Requires glycerol 3-phosphate and the GlpP product;
CC       repressed by glucose. {ECO:0000269|PubMed:1809833}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; M34393; AAA22487.1; -; Genomic_DNA.
DR   EMBL; Y14079; CAA74430.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12758.2; -; Genomic_DNA.
DR   PIR; C45868; C45868.
DR   RefSeq; NP_388811.2; NC_000964.3.
DR   RefSeq; WP_003233382.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P18158; -.
DR   SMR; P18158; -.
DR   STRING; 224308.BSU09300; -.
DR   jPOST; P18158; -.
DR   PaxDb; P18158; -.
DR   PRIDE; P18158; -.
DR   EnsemblBacteria; CAB12758; CAB12758; BSU_09300.
DR   GeneID; 936250; -.
DR   KEGG; bsu:BSU09300; -.
DR   PATRIC; fig|224308.179.peg.1003; -.
DR   eggNOG; COG0578; Bacteria.
DR   InParanoid; P18158; -.
DR   OMA; CIVNAAG; -.
DR   PhylomeDB; P18158; -.
DR   BioCyc; BSUB:BSU09300-MON; -.
DR   UniPathway; UPA00618; UER00674.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..555
FT                   /note="Aerobic glycerol-3-phosphate dehydrogenase"
FT                   /id="PRO_0000126097"
FT   BINDING         24..52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        385..386
FT                   /note="EH -> DD (in Ref. 1; AAA22487 and 2; CAA74430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   555 AA;  62568 MW;  A4181ACBC7E7F87A CRC64;
     MMNHQFSSLE RDRMLTDMTK KTYDLFIIGG GITGAGTALD AASRGMKVAL SEMQDFAAGT
     SSRSTKLVHG GLRYLKQFEV KMVAEVGKER AIVYENGPHV TTPEWMLLPF HKGGTFGSFT
     TSIGLRVYDF LAGVKKSERR SMLSAKETLQ KEPLVKKDGL KGGGYYVEYR TDDARLTIEV
     MKEAVKFGAE PVNYSKVKEL LYEKGKAVGV LIEDVLTKKE YKVYAKKIVN ATGPWVDQLR
     EKDHSKNGKH LQHTKGIHLV FDQSVFPLKQ AVYFDTPDGR MVFAIPREGK TYVGTTDTVY
     KEALEHPRMT TEDRDYVIKS INYMFPELNI TANDIESSWA GLRPLIHEEG KDPSEISRKD
     EIWTSDSGLI TIAGGKLTGY RKMAEHIVDL VRDRLKEEGE KDFGPCKTKN MPISGGHVGG
     SKNLMSFVTA KTKEGIAAGL SEKDAKQLAI RYGSNVDRVF DRVEALKDEA AKRNIPVHIL
     AEAEYSIEEE MTATPADFFV RRTGRLFFDI NWVRTYKDAV IDFMSERFQW DEQAKNKHTE
     NLNKLLHDAV VPLEQ