CAIB_ESCF3
ID CAIB_ESCF3 Reviewed; 405 AA.
AC B7LWM9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=EFER_0046;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
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; CU928158; CAQ87632.1; -; Genomic_DNA.
DR RefSeq; WP_000349959.1; NC_011740.1.
DR AlphaFoldDB; B7LWM9; -.
DR SMR; B7LWM9; -.
DR EnsemblBacteria; CAQ87632; CAQ87632; EFER_0046.
DR KEGG; efe:EFER_0046; -.
DR HOGENOM; CLU_033975_2_0_6; -.
DR OMA; HRPGFGT; -.
DR OrthoDB; 969868at2; -.
DR BioCyc; EFER585054:EFER_RS00480-MON; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000745; 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_1000136253"
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; 45059 MW; 799BBFE315DA2D65 CRC64;
MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
LAALHKVRET SKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMTKGKD PYYAGCGLYK
CADGYIVMEL VGITQIAECF KDIGLAHLLG TPEIPEGTQL IHRIECSYGP LVEEKLDAWL
AAHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNVMPKF
KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
