CAIA_PROSL
ID CAIA_PROSL Reviewed; 380 AA.
AC Q8GB20;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
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};
OS Proteus sp. (strain LE138).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=217617;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Engemann C., Elssner T., Pfeifer S., Krumbholz C., Maier T., Kleber H.-P.;
RT "Cai locus and corresponding enzymes of Proteus sp.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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; AJ508908; CAD48579.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GB20; -.
DR SMR; Q8GB20; -.
DR BRENDA; 1.3.8.13; 5048.
DR UniPathway; UPA00117; -.
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.
FT CHAIN 1..380
FT /note="Crotonobetainyl-CoA reductase"
FT /id="PRO_0000201196"
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
