(data stored in ACNUC7421 zone)

SWISSPROT: CAIC_ECO57

ID   CAIC_ECO57              Reviewed;         517 AA.
AC   Q8XA34;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   05-JUL-2017, entry version 91.
DE   RecName: Full=Probable crotonobetaine/carnitine-CoA ligase {ECO:0000255|HAMAP-Rule:MF_01524};
DE            EC=6.2.1.- {ECO:0000255|HAMAP-Rule:MF_01524};
GN   Name=caiC {ECO:0000255|HAMAP-Rule:MF_01524};
GN   OrderedLocusNames=Z0043, ECs0040;
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: Could catalyze the transfer of CoA to carnitine,
CC       generating the initial carnitinyl-CoA needed for the CaiB reaction
CC       cycle. {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG54340.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB33463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG54340.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33463.1; ALT_INIT; Genomic_DNA.
DR   PIR; H85484; H85484.
DR   PIR; H90633; H90633.
DR   RefSeq; NP_308067.2; NC_002695.1.
DR   RefSeq; WP_001301863.1; NZ_MWVM01000003.1.
DR   ProteinModelPortal; Q8XA34; -.
DR   SMR; Q8XA34; -.
DR   STRING; 155864.Z0043; -.
DR   PRIDE; Q8XA34; -.
DR   EnsemblBacteria; AAG54340; AAG54340; Z0043.
DR   EnsemblBacteria; BAB33463; BAB33463; BAB33463.
DR   GeneID; 913437; -.
DR   KEGG; ece:Z0043; -.
DR   KEGG; ecs:ECs0040; -.
DR   PATRIC; fig|386585.9.peg.137; -.
DR   eggNOG; ENOG4105CEY; Bacteria.
DR   eggNOG; COG0318; LUCA.
DR   HOGENOM; HOG000230001; -.
DR   KO; K02182; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:InterPro.
DR   GO; GO:0051108; F:carnitine-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0051109; F:crotonobetaine-CoA ligase activity; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01524; CaiC; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR023456; CaiC.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XA34.
DR   SWISS-2DPAGE; Q8XA34.
KW   Complete proteome; Ligase.
FT   CHAIN         1    517       Probable crotonobetaine/carnitine-CoA
FT                                ligase.
FT                                /FTId=PRO_0000193067.
SQ   SEQUENCE   517 AA;  58614 MW;  0B0778C5D1A40651 CRC64;
     MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
     KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE SAWILQNSQA CLLVTSAQFY
     PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
     ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP PSANDRQHRL REVMFYLNLS
     EQEKDTFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRAGFCYD AEIRDDHNRP
     LPAGEIGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFIDRR
     CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
     FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
//

If you have problems or comments...

PBIL Back to PBIL home page