CAIC_ECO45
ID CAIC_ECO45 Reviewed; 517 AA.
AC B7MAG0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 67.
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=ECS88_0040;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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=CAR01406.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU928161; CAR01406.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001514435.1; NC_011742.1.
DR AlphaFoldDB; B7MAG0; -.
DR SMR; B7MAG0; -.
DR EnsemblBacteria; CAR01406; CAR01406; ECS88_0040.
DR KEGG; ecz:ECS88_0040; -.
DR HOGENOM; CLU_000022_59_0_6; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000000747; 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_0000383399"
SQ SEQUENCE 517 AA; 58522 MW; 5F3E21CEC7AB5B12 CRC64;
MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE STWILQNSQA CLLVTSAQFY
PMYQQIQQED ASQLRHICLI DMALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
ATFVLVEKYS ARAFWGQVQK YRATITECIP MMIRTLMVQP PSANDRQHRL REVMFYLNLS
EQEKDAFCER FGVSLLTSYG MTETIVGIIG DRPGDKRRWP SIGRAGFCYE AEIRDDHNRP
LPAGELGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFVDRR
CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
FCFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK