ID   Q188I5_CLOD6            Unreviewed;       377 AA.
AC   Q188I5;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Acyl-CoA dehydrogenase, short-chain specific {ECO:0000313|EMBL:CAJ67220.1};
DE            EC=1.3.99.- {ECO:0000313|EMBL:CAJ67220.1};
GN   Name=acdB {ECO:0000313|EMBL:CAJ67220.1};
GN   OrderedLocusNames=CD630_03990 {ECO:0000313|EMBL:CAJ67220.1};
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ67220.1, ECO:0000313|Proteomes:UP000001978};
RN   [1] {ECO:0000313|EMBL:CAJ67220.1, ECO:0000313|Proteomes:UP000001978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630 {ECO:0000313|EMBL:CAJ67220.1,
RC   ECO:0000313|Proteomes:UP000001978};
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; AM180355; CAJ67220.1; -; Genomic_DNA.
DR   RefSeq; WP_003427762.1; NZ_JAUPES010000001.1.
DR   RefSeq; YP_001086865.1; NC_009089.1.
DR   AlphaFoldDB; Q188I5; -.
DR   SMR; Q188I5; -.
DR   STRING; 272563.CD630_03990; -.
DR   EnsemblBacteria; CAJ67220; CAJ67220; CD630_03990.
DR   GeneID; 66352924; -.
DR   KEGG; cdf:CD630_03990; -.
DR   KEGG; pdc:CDIF630_00527; -.
DR   PATRIC; fig|272563.120.peg.419; -.
DR   eggNOG; COG1960; Bacteria.
DR   OrthoDB; 9802447at2; -.
DR   PhylomeDB; Q188I5; -.
DR   BioCyc; PDIF272563:G12WB-505-MONOMER; -.
DR   Proteomes; UP000001978; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001978}.
FT   DOMAIN          5..116
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          120..215
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          227..375
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   377 AA;  40864 MW;  8F7D8D213408B324 CRC64;
     MLYNKEQELL RKAVRDFVSK ELDTLPAEMD KTGVMPKELI KKLADAKFIS SNIPEEYGGG
     GAGYVSYAIV MEEIARRCAS TATFVTAGSS LASLPILYNG TEEQKQKYLK GIATGELIGA
     FGLTEPGAGS DAGGQQTTAE LVGDHYILNG RKTFITNGPF CDVAIVIAVT DRSKGLRGTS
     AFIVESKWDG FSTGAHEDKM GIRGTETSDL IFENVKVPKE NLLGKEGQGF KIAMGTLEVG
     RIGVAALALG IAQGALDEAV KYTKQRVQFG KPIAKFQNTQ FTIADMETKV CAARGLVYDA
     AQKRDAGMRV AQESAMAKYY ASEIANEVAY KALQLHGGYG FIKDYEIERM YRDARIVSIY
     EGTSEVQKMV ISSNVLK
//