ID   CAIB_ECOBW              Reviewed;         405 AA.
AC   C4ZPW4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=BWG_0036;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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; CP001396; ACR62673.1; -; Genomic_DNA.
DR   RefSeq; WP_000349936.1; NC_012759.1.
DR   AlphaFoldDB; C4ZPW4; -.
DR   SMR; C4ZPW4; -.
DR   KEGG; ebw:BWG_0036; -.
DR   HOGENOM; CLU_033975_2_0_6; -.
DR   OMA; HRPGFGT; -.
DR   UniPathway; UPA00117; -.
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_1000213430"
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;  45127 MW;  75583684B4B5A2DE CRC64;
     MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
     LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
     AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
     LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK
     CADGYIVMEL VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
     ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED