ID   CAIC_SALPK              Reviewed;         517 AA.
AC   B5BL55;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=SSPA0068;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(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; FM200053; CAR58179.1; -; Genomic_DNA.
DR   RefSeq; WP_000355788.1; NC_011147.1.
DR   AlphaFoldDB; B5BL55; -.
DR   SMR; B5BL55; -.
DR   KEGG; sek:SSPA0068; -.
DR   HOGENOM; CLU_000022_59_0_6; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001869; 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_1000200920"
SQ   SEQUENCE   517 AA;  58248 MW;  D99D52B7BF0B72E4 CRC64;
     MDIVGGQNLR QMWDDLAEVY GDKTALIFES CEGIVRQFSY ASLNEEINRT ANLFHSLGIR
     KGDRVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLGEE SAWILQNSQV SLLVTSAQFY
     PMYREIRQGN STPLNHICLI GEQLPADDGV SLFSQLQARQ SATLCYTPAL STDDAAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQIA LRDDDVYMTV MPAFHIDCQC TAAMPAFSAG
     STFVLLEKYS ARAFWGQVRK YQATVTECIP MMIRTLMVQP AAPTDRQHHL REVMFYLNLS
     AQEKDAFTER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFSYE AEIRDDQNRP
     LPAGEIGEIC IKGIPGKTIF KEYYMQPEAT ARALEPEGWL HTGDSGYQDE DGYFYFVDRR
     CNMIKRGGEN VSCVELENII SAHPKIQDIV VVGIKDAIRD EAIKAFIVLN EGETLSEAEF
     FSFCENNMAK FKVPSFMEIR TDLPRNCSGK IIKKNLK