ID   CAIC_ECOUT              Reviewed;         517 AA.
AC   Q1RGG1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   25-MAY-2022, entry version 79.
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}; OrderedLocusNames=UTI89_C0043;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Catalyzes the transfer of CoA to carnitine, generating the
CC       initial carnitinyl-CoA needed for the CaiB reaction cycle. Also has
CC       activity toward crotonobetaine and gamma-butyrobetaine.
CC       {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-(trimethylamino)butanoate + ATP + CoA = AMP + diphosphate +
CC         gamma-butyrobetainyl-CoA; Xref=Rhea:RHEA:55960, ChEBI:CHEBI:16244,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:61513, ChEBI:CHEBI:456215; EC=6.2.1.48;
CC         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 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01524}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE05553.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000243; ABE05553.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001350362.1; NC_007946.1.
DR   AlphaFoldDB; Q1RGG1; -.
DR   SMR; Q1RGG1; -.
DR   EnsemblBacteria; ABE05553; ABE05553; UTI89_C0043.
DR   KEGG; eci:UTI89_C0043; -.
DR   HOGENOM; CLU_000022_59_0_6; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001952; 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; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   HAMAP; MF_01524; CaiC; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_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;
KW   Ligase.
FT   CHAIN           1..517
FT                   /note="Crotonobetaine/carnitine--CoA ligase"
FT                   /id="PRO_0000298679"
SQ   SEQUENCE   517 AA;  58591 MW;  D4845015289EC4B9 CRC64;
     MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
     KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE STWILQNSQA CLLVTSAQFY
     PMYQQIQQED ASQLRHICLI DMALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
     ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP PSANDRQHRL REVMFYLNLS
     EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRAGFCYE AEIRDDHNRP
     LPAGELGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFVDRR
     CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
     FCFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK