ID   CAIB_ECO81              Reviewed;         405 AA.
AC   B7MNP5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=L-carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
DE            EC=2.8.3.21 {ECO:0000255|HAMAP-Rule:MF_01050};
DE   AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
GN   Name=caiB {ECO:0000255|HAMAP-Rule:MF_01050}; OrderedLocusNames=ECED1_0037;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the CoA moiety from
CC       gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA
CC       and gamma-butyrobetaine. Is also able to catalyze the reversible
CC       transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-
CC       carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA.
CC       {ECO:0000255|HAMAP-Rule:MF_01050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + crotonobetainyl-CoA = (R)-carnitinyl-CoA +
CC         crotonobetaine; Xref=Rhea:RHEA:28526, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:17237, ChEBI:CHEBI:60932, ChEBI:CHEBI:60933; EC=2.8.3.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01050};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + gamma-butyrobetainyl-CoA = (R)-carnitinyl-CoA
CC         + 4-(trimethylamino)butanoate; Xref=Rhea:RHEA:28418,
CC         ChEBI:CHEBI:16244, ChEBI:CHEBI:16347, ChEBI:CHEBI:60932,
CC         ChEBI:CHEBI:61513; EC=2.8.3.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01050};
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01050}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01050}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01050}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01050}.
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DR   EMBL; CU928162; CAR06260.1; -; Genomic_DNA.
DR   RefSeq; WP_000349942.1; NC_011745.1.
DR   AlphaFoldDB; B7MNP5; -.
DR   SMR; B7MNP5; -.
DR   EnsemblBacteria; CAR06260; CAR06260; ECED1_0037.
DR   KEGG; ecq:ECED1_0037; -.
DR   HOGENOM; CLU_033975_2_0_6; -.
DR   OMA; HRPGFGT; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008410; F:CoA-transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   HAMAP; MF_01050; CaiB; 1.
DR   InterPro; IPR023452; CoA-Trfase_CaiB.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Transferase.
FT   CHAIN           1..405
FT                   /note="L-carnitine CoA-transferase"
FT                   /id="PRO_1000149624"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT   BINDING         97
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT   BINDING         104
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
SQ   SEQUENCE   405 AA;  45053 MW;  275835C6A38B62F9 CRC64;
     MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
     LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
     AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
     LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMTKGKD PYYAGCGLYK
     CADGYIVMEL VGITQIAECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
     AAHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED