CAIC_ECO57
ID CAIC_ECO57 Reviewed; 517 AA.
AC Q8XA34;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
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};
GN OrderedLocusNames=Z0043, ECs0040;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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=AAG54340.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB33463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG54340.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB33463.1; ALT_INIT; Genomic_DNA.
DR PIR; H85484; H85484.
DR PIR; H90633; H90633.
DR RefSeq; NP_308067.2; NC_002695.1.
DR RefSeq; WP_001301863.1; NZ_SEKU01000001.1.
DR AlphaFoldDB; Q8XA34; -.
DR SMR; Q8XA34; -.
DR STRING; 155864.EDL933_0038; -.
DR EnsemblBacteria; AAG54340; AAG54340; Z0043.
DR EnsemblBacteria; BAB33463; BAB33463; ECs_0040.
DR GeneID; 913437; -.
DR KEGG; ece:Z0043; -.
DR KEGG; ecs:ECs_0040; -.
DR PATRIC; fig|386585.9.peg.137; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_6; -.
DR OMA; WLMQRAF; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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..517
FT /note="Crotonobetaine/carnitine--CoA ligase"
FT /id="PRO_0000193067"
SQ SEQUENCE 517 AA; 58614 MW; 0B0778C5D1A40651 CRC64;
MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE SAWILQNSQA CLLVTSAQFY
PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP PSANDRQHRL REVMFYLNLS
EQEKDTFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRAGFCYD AEIRDDHNRP
LPAGEIGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFIDRR
CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
