(data stored in ACNUC7421 zone)

SWISSPROT: CAIC_ECO27

ID   CAIC_ECO27              Reviewed;         517 AA.
AC   B7UI83;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Crotonobetaine/carnitine--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01524};
DE            EC=6.2.1.48 {ECO:0000255|HAMAP-Rule:MF_01524};
GN   Name=caiC {ECO:0000255|HAMAP-Rule:MF_01524};
GN   OrderedLocusNames=E2348C_0038;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the transfer of CoA to carnitine, generating
CC       the initial carnitinyl-CoA needed for the CaiB reaction cycle.
CC       Also has activity toward crotonobetaine and gamma-butyrobetaine.
CC       {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(trimethylamino)butanoate + ATP + CoA = AMP +
CC         diphosphate + gamma-butyrobetainyl-CoA; Xref=Rhea:RHEA:55960,
CC         ChEBI:CHEBI:16244, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:61513, ChEBI:CHEBI:456215;
CC         EC=6.2.1.48; Evidence={ECO:0000255|HAMAP-Rule:MF_01524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + crotonobetaine = AMP + crotonobetainyl-CoA +
CC         diphosphate; Xref=Rhea:RHEA:30079, ChEBI:CHEBI:17237,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:60933, ChEBI:CHEBI:456215; EC=6.2.1.48;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01524};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + ATP + CoA = (R)-carnitinyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:28514, ChEBI:CHEBI:16347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:60932, ChEBI:CHEBI:456215; EC=6.2.1.48;
CC         Evidence={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}.
DR   EMBL; FM180568; CAS07586.1; -; Genomic_DNA.
DR   RefSeq; WP_012578833.1; NC_011601.1.
DR   SMR; B7UI83; -.
DR   PRIDE; B7UI83; -.
DR   EnsemblBacteria; CAS07586; CAS07586; E2348C_0038.
DR   KEGG; ecg:E2348C_0038; -.
DR   KO; K02182; -.
DR   OMA; WLMQRAF; -.
DR   BioCyc; ECOL574521:E2348C_RS00200-MONOMER; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008205; 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   Gene3D; 3.40.50.12780; -; 1.
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; IPR042099; AMP-dep_Synthh-like_sf.
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; B7UI83.
DR   SWISS-2DPAGE; B7UI83.
KW   Complete proteome; Ligase.
FT   CHAIN         1    517       Crotonobetaine/carnitine--CoA ligase.
FT                                /FTId=PRO_1000185129.
SQ   SEQUENCE   517 AA;  58613 MW;  F3EF90CAD35CC516 CRC64;
     MDIIGGQHLR QMWDDLADVY GHKTALICES SSGVVNRYSY LELNQEINRT ANLFYTLGIR
     KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE STWILQNSQA CLLVTSAQFY
     PMYQQIQQED ATQLRHICLT DVSLPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSTG
     ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP LSANDQQHRL REVMFYLNLS
     EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGQAGFCYE AEIRDDHNRP
     LPAGEIGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFVDRR
     CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
     FCFCEQNMAK FKVLSYLEIR KDLPRNCSGK IIRKNLK
//

If you have problems or comments...

PBIL Back to PBIL home page