ID   CAIC_SALA4              Reviewed;         517 AA.
AC   B5F750;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=SeAg_B0078;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH48610.1; -; Genomic_DNA.
DR   RefSeq; WP_000355808.1; NC_011149.1.
DR   AlphaFoldDB; B5F750; -.
DR   SMR; B5F750; -.
DR   EnsemblBacteria; ACH48610; ACH48610; SeAg_B0078.
DR   KEGG; sea:SeAg_B0078; -.
DR   HOGENOM; CLU_000022_59_0_6; -.
DR   OMA; WLMQRAF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008819; 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_1000200915"
SQ   SEQUENCE   517 AA;  58534 MW;  00C4FA7CA2D0F67D CRC64;
     MDIVGGQNLR QMWDDLAGVY GDKTALIFES CEGIVRQFSY ASLNEEINRT ANLFYSLGIR
     KGDRVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLGEE SAWILQNSQV SLLVTSAQFY
     PMYREIRQDN STPLNHICLI GEQLPADDGV SHFTQLQSRQ STTLCYTPAL STDDTAEILF
     TSGTTSRPKG VVITHYNLRF AGYYSAWQIA LRDDDVYMTV MPAFHIDCQC TAAMPAFSAG
     STFVLLEKYS ARAFWDQVRK YQATVTECIP MMIRTLMVQP AAPTDRQHHL REVMFYLNLS
     EQEKDDFTER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFSYE AEIRDDQNRP
     LPAGEIGEIC IKGIPGKTIF KEYYMQPEAT ARALEPEGWL HTGDSGYQDE DGYFYFVDRR
     CNMIKRGGEN VSCVELENII SAHPKIQDIV VVGIKDAIRD EAIKAFIVLN EGETLSEAEF
     FSFCENNMAK FKVPSFMEIR TDLPRNCSGK IIKKNLK