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 03-AUG-2022, entry version 118.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P96608; -.
DR SMR; P96608; -.
DR STRING; 224308.BSU04520; -.
DR PaxDb; P96608; -.
DR PRIDE; P96608; -.
DR EnsemblBacteria; CAB12259; CAB12259; BSU_04520.
DR GeneID; 939949; -.
DR KEGG; bsu:BSU04520; -.
DR PATRIC; fig|224308.179.peg.479; -.
DR eggNOG; COG1960; Bacteria.
DR InParanoid; P96608; -.
DR OMA; NPPMDDM; -.
DR PhylomeDB; P96608; -.
DR BioCyc; BSUB:BSU04520-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..381
FT /note="Putative acyl-CoA dehydrogenase YdbM"
FT /id="PRO_0000360817"
FT BINDING 158..160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 337..341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
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
