(data stored in ACNUC7421 zone)

SWISSPROT: CAIB_ECO57

ID   CAIB_ECO57              Reviewed;         405 AA.
AC   Q8XA32;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 111.
DE   RecName: Full=L-carnitine CoA-transferase;
DE            EC=2.8.3.21;
DE   AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase;
GN   Name=caiB; OrderedLocusNames=Z0044, ECs0041;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the CoA moiety from
CC       gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-
CC       CoA and gamma-butyrobetaine. Is also able to catalyze the
CC       reversible transfer of the CoA moiety from gamma-butyrobetainyl-
CC       CoA or L-carnitinyl-CoA to crotonobetaine to generate
CC       crotonobetainyl-CoA (By similarity). {ECO:0000250}.
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;
CC         EC=2.8.3.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + gamma-butyrobetainyl-CoA = (R)-
CC         carnitinyl-CoA + 4-(trimethylamino)butanoate;
CC         Xref=Rhea:RHEA:28418, ChEBI:CHEBI:16244, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:60932, ChEBI:CHEBI:61513; EC=2.8.3.21;
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CaiB/BaiF CoA-transferase family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG54341.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33464.1; -; Genomic_DNA.
DR   PIR; A85485; A85485.
DR   PIR; A90634; A90634.
DR   RefSeq; NP_308068.1; NC_002695.1.
DR   RefSeq; WP_000349922.1; NZ_SDVX01000001.1.
DR   SMR; Q8XA32; -.
DR   STRING; 155864.EDL933_0039; -.
DR   EnsemblBacteria; AAG54341; AAG54341; Z0044.
DR   EnsemblBacteria; BAB33464; BAB33464; BAB33464.
DR   GeneID; 913438; -.
DR   KEGG; ece:Z0044; -.
DR   KEGG; ecs:ECs0041; -.
DR   PATRIC; fig|386585.9.peg.138; -.
DR   eggNOG; ENOG4105C04; Bacteria.
DR   eggNOG; COG1804; LUCA.
DR   HOGENOM; HOG000219745; -.
DR   KO; K08298; -.
DR   BioCyc; ECOO157:CAIB-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Q8XA32.
DR   SWISS-2DPAGE; Q8XA32.
KW   Complete proteome; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN         1    405       L-carnitine CoA-transferase.
FT                                /FTId=PRO_0000194709.
FT   ACT_SITE    169    169       Nucleophile. {ECO:0000250}.
FT   BINDING      97     97       Coenzyme A. {ECO:0000250}.
FT   BINDING     104    104       Coenzyme A. {ECO:0000250}.
SQ   SEQUENCE   405 AA;  45069 MW;  1B83CEED545CD2BA CRC64;
     MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
     LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
     AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
     LAALHKARET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK
     CADGYIVMEL VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
     AAHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
     KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
//

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