(data stored in ACNUC7421 zone)

SWISSPROT: YDBM_BACSU

ID   YDBM_BACSU              Reviewed;         381 AA.
AC   P96608; Q797L3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Putative acyl-CoA dehydrogenase YdbM;
DE            EC=1.3.99.-;
GN   Name=ydbM; OrderedLocusNames=BSU04520;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT   "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT   subtilis genome.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   INDUCTION.
RX   PubMed=16513748; DOI=10.1128/jb.188.6.2184-2197.2006;
RA   Even S., Burguiere P., Auger S., Soutourina O., Danchin A.,
RA   Martin-Verstraete I.;
RT   "Global control of cysteine metabolism by CymR in Bacillus subtilis.";
RL   J. Bacteriol. 188:2184-2197(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- INDUCTION: Induced by methionine. Repressed by sulfate via the cysteine
CC       metabolism repressor YrzC/CymR. {ECO:0000269|PubMed:16513748}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
DR   EMBL; AB001488; BAA19289.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12259.1; -; Genomic_DNA.
DR   PIR; H69771; H69771.
DR   RefSeq; NP_388333.1; NC_000964.3.
DR   RefSeq; WP_003234334.1; NZ_JNCM01000031.1.
DR   SMR; P96608; -.
DR   STRING; 224308.BSU04520; -.
DR   PaxDb; P96608; -.
DR   PRIDE; P96608; -.
DR   EnsemblBacteria; CAB12259; CAB12259; BSU04520.
DR   GeneID; 939949; -.
DR   KEGG; bsu:BSU04520; -.
DR   PATRIC; fig|224308.179.peg.479; -.
DR   eggNOG; ENOG4105FDT; Bacteria.
DR   eggNOG; ENOG410XWKU; LUCA.
DR   HOGENOM; HOG000131663; -.
DR   InParanoid; P96608; -.
DR   OMA; NPPMDDM; -.
DR   PhylomeDB; P96608; -.
DR   BioCyc; BSUB:BSU04520-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   InterPro; IPR013107; Acyl-CoA_DH_C_dom.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P96608.
DR   SWISS-2DPAGE; P96608.
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Putative acyl-CoA dehydrogenase YdbM"
FT                   /id="PRO_0000360817"
FT   NP_BIND         158..160
FT                   /note="FAD"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         337..341
FT                   /note="FAD"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   381 AA;  42140 MW;  0EA6AD4545AA15ED CRC64;
     MSLFIQNDQQ RQWMEKIGRI ADEFQQTAAE DDEQGRFPAE KIQKLRDAGY TALTLPASHG
     GGGISVYDML LFQERLARGD APTALSIGWH LSVIGELGEG NSWDEDVFAF VAKEVQNGAV
     INRAATEAKT GSPTRGGRPG THAVKKDGKW AVNGRKTFTT MSQALDYFLV TAWIEDKQTT
     GVFLIHKDDP GLSIEETWDM MAMRATGSHD LVLNEVMLDE NKLVELLQGP RGAKPNGWLL
     HIPAIYLGVA QAARDYAVQF ASEYSPNSLN GPIKNVPAVQ QRTGEMELEL LNARHFLFHI
     AQLYDDPVRR PHLTSELGAA KHIVTNAALS VVDKAMRIVG AKSLERTNPL QRYYRDVRAG
     LHNPPMDDAV IHKLAAEAFE S
//

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