CAIC_ECOL6
ID CAIC_ECOL6 Reviewed; 517 AA.
AC Q8FLA5;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 83.
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=c0046;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN78544.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN78544.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001298634.1; NC_004431.1.
DR AlphaFoldDB; Q8FLA5; -.
DR SMR; Q8FLA5; -.
DR STRING; 199310.c0046; -.
DR EnsemblBacteria; AAN78544; AAN78544; c0046.
DR KEGG; ecc:c0046; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_6; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001410; 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_0000193066"
SQ SEQUENCE 517 AA; 58655 MW; C66E32D6A3BD27F6 CRC64;
MDIIGGQHLR QMWDDLADVY GHKTALICES SSGVVNRYSY LELNQEINRT ANLFYTLGIR
KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE STWILQNSQA CLLVTSAQFY
PMYQQIQQED ASQLRHICLT DMVLPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP LSANDQQHRL REVMFYLNLS
EQEKDAFCER FSVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRAGFCYE AEIRDDHNRP
LPAGELGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFVDRR
CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
FCFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK