(data stored in ACNUC7421 zone)

SWISSPROT: CAIB_ECOL5

ID   CAIB_ECOL5              Reviewed;         405 AA.
AC   Q0TLV1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 87.
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=ECP_0038;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
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}.
DR   EMBL; CP000247; ABG68080.1; -; Genomic_DNA.
DR   RefSeq; WP_000349956.1; NC_008253.1.
DR   SMR; Q0TLV1; -.
DR   EnsemblBacteria; ABG68080; ABG68080; ECP_0038.
DR   KEGG; ecp:ECP_0038; -.
DR   eggNOG; ENOG4105C04; Bacteria.
DR   eggNOG; COG1804; LUCA.
DR   HOGENOM; HOG000219745; -.
DR   KO; K08298; -.
DR   OMA; HRPGFGT; -.
DR   BioCyc; ECOL362663:G1G5S-41-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000009182; 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; 3.40.50.10540; -; 1.
DR   HAMAP; MF_01050; CaiB; 1.
DR   InterPro; IPR023452; CoA-Trfase_CaiB.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0TLV1.
DR   SWISS-2DPAGE; Q0TLV1.
KW   Cytoplasm; Transferase.
FT   CHAIN           1..405
FT                   /note="L-carnitine CoA-transferase"
FT                   /id="PRO_0000300980"
FT   ACT_SITE        169
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT   BINDING         97
FT                   /note="Coenzyme A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT   BINDING         104
FT                   /note="Coenzyme A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
SQ   SEQUENCE   405 AA;  45083 MW;  D2582197E9DB8CF8 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 VGITQITECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
     AAHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
//

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