ID   CAIC_PROMH              Reviewed;         518 AA.
AC   B4EY25;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=PMI2657;
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=529507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320;
RX   PubMed=18375554; DOI=10.1128/jb.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.T.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR45236.1; -; Genomic_DNA.
DR   RefSeq; WP_012368455.1; NC_010554.1.
DR   AlphaFoldDB; B4EY25; -.
DR   SMR; B4EY25; -.
DR   STRING; 529507.PMI2657; -.
DR   EnsemblBacteria; CAR45236; CAR45236; PMI2657.
DR   GeneID; 6803547; -.
DR   KEGG; pmr:PMI2657; -.
DR   PATRIC; fig|529507.6.peg.2585; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_6; -.
DR   OMA; AWPNTDF; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008319; 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; Reference proteome.
FT   CHAIN           1..518
FT                   /note="Crotonobetaine/carnitine--CoA ligase"
FT                   /id="PRO_1000200914"
SQ   SEQUENCE   518 AA;  58925 MW;  C06392C136768B9F CRC64;
     MDVIGRQHLR QMWDDLAEVY DKKTALIFES AQGKVRQFSY SELNEEINRA ANLFHACGIK
     KGDHVALHLD NCPEFFFCWF GLAKIGAVMV PINARFMYEE SAWIINHCQA HFVVTSDNFS
     PIYQPMLHDK HSPLTQLFLI TENCLPTEQG VVDFLSEKAK HPVTLNHHTP LSVDDTAEIL
     FTSGTTSQPK GVVITHYNLR FAGYYSSWQN ALREDDIYLT VMPAFHIDCQ CTASLPAFSV
     GATFVLLEKY SARAFWKQIL KYQATVTECI PMMMRTLMAQ PVSPDEKQHK LREVMFYLNL
     ADEEKDAFIE RFNVRLLTSY GMTETIVGLI GDRPGDKRRW PSIGRPGFCY QAQIRDKQNQ
     QVPNGVVGEI CVKGEPGKTL FKEYYNRPDA TEKALEPDGW LHTGDYGYQD DEGFFYFVDR
     SCNMIKRGGE NVSCIEIENI IASHPKIQDV AVIGVPDDIR DEAIKAFVVL VDGETLSEEA
     FFAFCEQNMA KFKVPSAVEF KQGLPRNCSG KVIKKHLQ