ID   CAIC_SALPC              Reviewed;         517 AA.
AC   C0Q4L3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=SPC_0076;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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}.
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DR   EMBL; CP000857; ACN44268.1; -; Genomic_DNA.
DR   RefSeq; WP_000355814.1; NC_012125.1.
DR   AlphaFoldDB; C0Q4L3; -.
DR   SMR; C0Q4L3; -.
DR   EnsemblBacteria; ACN44268; ACN44268; SPC_0076.
DR   KEGG; sei:SPC_0076; -.
DR   HOGENOM; CLU_000022_59_0_6; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001599; 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_1000185130"
SQ   SEQUENCE   517 AA;  58310 MW;  C9B1D675F56F3A91 CRC64;
     MDIVGGQNLR QMWDDLAGVY GDKTALIFES CEGIVRQFSY ASLNEEINRT ANLFYSLGIR
     KGDRVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLGEE SAWILQNSQV SLLVTSVQFY
     PMYREIHQDN STPLNHICLI GEQLPADDGV SHFSQLQARQ SATLCYTPAL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQIA LRDDDVYMTV MPAFHIDCQC TAAMPAFSAG
     STFVLLEKYS ARAFWDQVRR YQATVTECIP MMIRTLMVQP AAPTDRQHHL REVMFYLNLS
     AQEKDAFTER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFSYE AEIRDDQNRP
     LPAGEIGEIC IKGIPGKTIF KEYYMQPEAT AGALEPEGWL HTGDSGYQDE DGYFYFVDRR
     CNMIKRGGEN VSCVELENII SAHPKIQDIV VVGIKDAIRD EAIKAFIVLN EGETLSEAEF
     FSFCENNMAK FKVPSFMEIR TDLPRNCSGK IIKKNLK