CAIA_ECOLI
ID CAIA_ECOLI Reviewed; 380 AA.
AC P60584; P31571;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Crotonobetainyl-CoA reductase {ECO:0000255|HAMAP-Rule:MF_01052};
DE EC=1.3.8.13 {ECO:0000255|HAMAP-Rule:MF_01052, ECO:0000269|PubMed:10978161};
DE AltName: Full=Crotobetaine reductase {ECO:0000303|PubMed:8060125};
DE AltName: Full=Crotonobetainyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01052};
GN Name=caiA {ECO:0000255|HAMAP-Rule:MF_01052, ECO:0000303|PubMed:7815937};
GN Synonyms=yaaO; OrderedLocusNames=b0039, JW0038;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O44:K74;
RX PubMed=7815937; DOI=10.1111/j.1365-2958.1994.tb00470.x;
RA Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.;
RT "Molecular characterization of the cai operon necessary for carnitine
RT metabolism in Escherichia coli.";
RL Mol. Microbiol. 13:775-786(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 143
RP AND 182.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=O44:K74;
RX PubMed=8060125; DOI=10.1007/bf00878280;
RA Roth S., Jung K., Jung H., Hommel R.K., Kleber H.P.;
RT "Crotonobetaine reductase from Escherichia coli--a new inducible enzyme of
RT anaerobic metabolization of L(-)-carnitine.";
RL Antonie Van Leeuwenhoek 65:63-69(1994).
RN [6]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=O44:K74;
RX PubMed=10209289; DOI=10.1016/s0167-4838(99)00032-1;
RA Preusser A., Wagner U., Elssner T., Kleber H.-P.;
RT "Crotonobetaine reductase from Escherichia coli consists of two proteins.";
RL Biochim. Biophys. Acta 1431:166-178(1999).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=O44:K74;
RX PubMed=10978161; DOI=10.1021/bi000776c;
RA Elssner T., Hennig L., Frauendorf H., Haferburg D., Kleber H.P.;
RT "Isolation, identification, and synthesis of gamma-butyrobetainyl-CoA and
RT crotonobetainyl-CoA, compounds involved in carnitine metabolism of E.
RT coli.";
RL Biochemistry 39:10761-10769(2000).
RN [8]
RP FUNCTION.
RC STRAIN=K12 / BW25113;
RX PubMed=12081978; DOI=10.1128/jb.184.14.4044-4047.2002;
RA Walt A., Kahn M.L.;
RT "The fixA and fixB genes are necessary for anaerobic carnitine reduction in
RT Escherichia coli.";
RL J. Bacteriol. 184:4044-4047(2002).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=23718679; DOI=10.1186/1475-2859-12-56;
RA Arense P., Bernal V., Charlier D., Iborra J.L., Foulquie-Moreno M.R.,
RA Canovas M.;
RT "Metabolic engineering for high yielding L(-)-carnitine production in
RT Escherichia coli.";
RL Microb. Cell Fact. 12:56-56(2013).
CC -!- FUNCTION: Catalyzes the reduction of crotonobetainyl-CoA to gamma-
CC butyrobetainyl-CoA (PubMed:8060125, PubMed:10209289, PubMed:10978161).
CC The electron donor could be the FixA/FixB complex (PubMed:12081978).
CC {ECO:0000269|PubMed:10978161, ECO:0000269|PubMed:12081978,
CC ECO:0000305|PubMed:10209289, ECO:0000305|PubMed:8060125}.
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 ECO:0000269|PubMed:10978161};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01052,
CC ECO:0000269|PubMed:10209289};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10209289};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:8060125};
CC Temperature dependence:
CC Optimum temperature is 40-45 degrees Celsius.
CC {ECO:0000269|PubMed:8060125};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01052, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01052,
CC ECO:0000269|PubMed:10209289}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01052,
CC ECO:0000269|PubMed:8060125}.
CC -!- INDUCTION: Transcribed during anaerobic growth in the presence of L-
CC carnitine or crotonobetaine. {ECO:0000269|PubMed:7815937,
CC ECO:0000269|PubMed:8060125}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes gamma-
CC butyrobetaine formation and increases L-carnitine production under
CC anaerobic and aerobic conditions. {ECO:0000269|PubMed:23718679}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01052, ECO:0000305}.
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DR EMBL; X73904; CAA52111.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73150.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96608.2; -; Genomic_DNA.
DR PIR; G64724; I41011.
DR RefSeq; NP_414581.1; NC_000913.3.
DR RefSeq; WP_000347117.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P60584; -.
DR SMR; P60584; -.
DR BioGRID; 4263349; 362.
DR DIP; DIP-9241N; -.
DR IntAct; P60584; 5.
DR STRING; 511145.b0039; -.
DR PaxDb; P60584; -.
DR PRIDE; P60584; -.
DR EnsemblBacteria; AAC73150; AAC73150; b0039.
DR EnsemblBacteria; BAB96608; BAB96608; BAB96608.
DR GeneID; 67416114; -.
DR GeneID; 949064; -.
DR KEGG; ecj:JW0038; -.
DR KEGG; eco:b0039; -.
DR PATRIC; fig|1411691.4.peg.2244; -.
DR EchoBASE; EB1521; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_6; -.
DR InParanoid; P60584; -.
DR OMA; CFITNSG; -.
DR PhylomeDB; P60584; -.
DR BioCyc; EcoCyc:CROBETREDUCT-MON; -.
DR BioCyc; MetaCyc:CROBETREDUCT-MON; -.
DR BRENDA; 1.3.8.13; 2026.
DR UniPathway; UPA00117; -.
DR PRO; PR:P60584; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
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 GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..380
FT /note="Crotonobetainyl-CoA reductase"
FT /id="PRO_0000201193"
SQ SEQUENCE 380 AA; 42558 MW; 7076984D735652C3 CRC64;
MDFNLNDEQE LFVAGIRELM ASENWEAYFA ECDRDSVYPE RFVKALADMG IDSLLIPEEH
GGLDAGFVTL AAVWMELGRL GAPTYVLYQL PGGFNTFLRE GTQEQIDKIM AFRGTGKQMW
NSAITEPGAG SDVGSLKTTY TRRNGKIYLN GSKCFITSSA YTPYIVVMAR DGASPDKPVY
TEWFVDMSKP GIKVTKLEKL GLRMDSCCEI TFDDVELDEK DMFGREGNGF NRVKEEFDHE
RFLVALTNYG TAMCAFEDAA RYANQRVQFG EAIGRFQLIQ EKFAHMAIKL NSMKNMLYEA
AWKADNGTIT SGDAAMCKYF CANAAFEVVD SAMQVLGGVG IAGNHRISRF WRDLRVDRVS
GGSDEMQILT LGRAVLKQYR
