ID   CAIA_PROMH              Reviewed;         380 AA.
AC   B4EY23;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Crotonobetainyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_01052};
DE            EC=1.3.8.13 {ECO:0000255|HAMAP-Rule:MF_01052};
DE   AltName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01052};
GN   Name=caiA {ECO:0000255|HAMAP-Rule:MF_01052}; OrderedLocusNames=PMI2655;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Catalyzes the reduction of crotonobetainyl-CoA to gamma-
CC       butyrobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-butyrobetainyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = crotonobetainyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:51584, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:60933, ChEBI:CHEBI:61513; EC=1.3.8.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01052};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01052};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01052}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01052}.
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DR   EMBL; AM942759; CAR45233.1; -; Genomic_DNA.
DR   RefSeq; WP_004245793.1; NC_010554.1.
DR   AlphaFoldDB; B4EY23; -.
DR   SMR; B4EY23; -.
DR   STRING; 529507.PMI2655; -.
DR   EnsemblBacteria; CAR45233; CAR45233; PMI2655.
DR   GeneID; 6803562; -.
DR   KEGG; pmr:PMI2655; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   OMA; WACESMI; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   HAMAP; MF_01052; CaiA; 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.
DR   InterPro; IPR023450; CaiA.
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   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Crotonobetainyl-CoA reductase"
FT                   /id="PRO_1000136277"
SQ   SEQUENCE   380 AA;  42837 MW;  D49F2D25C394CC3A CRC64;
     MDFRLNDEQE LFVDGVRELM ASENWEAYFA QCDRESKYPE RFVKALADME IDNLLIPEEH
     GGLNAGFVTV AAIWMELGRL GAPTYVLYQL PGGFNTVLRE GTQEQIDKIM AFRGTGKQMW
     NSAITEPGAG SDVGSLQTTY TRKNGKVYLN GSKCFITSSA YTPYIVVMSR DAASPDKPIF
     TEWFVDMSKP GIKVTKLEKL GLRMDSCCEI TFDNVELEEK DMFGREGNGF NRVKEEFDHE
     RFLVALTNYG TAMCAFEDAA RYANQRVQFG ETIGRFQLIQ EKFAHMAIKL NSMRNMLYET
     AWKSDNGLIT SGDAAMCKYF CANAAFEVVD SAMQVLGGVG IAGEHRIARF WRDLRVDRVS
     GGSDEMQILT LGRAVLKQYR