ID   CAIC_PROSL              Reviewed;         518 AA.
AC   Q8GB18;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 50.
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};
OS   Proteus sp. (strain LE138).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=217617;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Engemann C., Elssner T., Pfeifer S., Krumbholz C., Maier T., Kleber H.-P.;
RT   "Cai locus and corresponding enzymes of Proteus sp.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
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; AJ508908; CAD48581.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GB18; -.
DR   SMR; Q8GB18; -.
DR   BRENDA; 6.2.1.48; 5048.
DR   UniPathway; UPA00117; -.
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..518
FT                   /note="Crotonobetaine/carnitine--CoA ligase"
FT                   /id="PRO_0000193068"
SQ   SEQUENCE   518 AA;  58608 MW;  F97B6FE2221EFAF9 CRC64;
     MDVIGRQHLR QMWDDLAEVY DKKTALIFES AQGKVRQFSY SELNEEINRA ANLFHACGIK
     KGDHVALHLD NCPEFFFCWF GLAKIGAVMV PINARFMYEE SAWIINHCQA HFVVTSDNFS
     PIYQPMLHDK HSPLTQLFLI TENCLPTEQG VVDFLSEKAK HPVTLNHHTP LSVDDTAEIL
     FTSGTTSQPK GVVITHYNLR IAGYYSSWQN ALREDDIYLT VMPAFHIDCQ CTASLPAYSV
     GATIVLLEKY SARASWKQIL KYQATVTECI PMMMRTSMAQ PVSPDEKQHK LREVMSYLNL
     ADKEKDASIE RLNVRLLTSH GMTETIVGLI GDRPGDKRRW PSIGRPGFCY QAQIRDKQNQ
     QVPNGVVGEI CVKGEAGKTL FKEYYNRPDA TEKALEPDGW LHTGDYGYRD DEGFFYFVDR
     SCNMIKRGGE NVSCIEIENI IASHPKIQDV AVIGVPDDIR DEAIKAFVVL VDGETLSEEA
     FFAFCEQNMA KFKVPSAVEF KQGLPRNCSG KVIKKHLQ