CAIC_ECOLI
ID CAIC_ECOLI Reviewed; 517 AA.
AC P31552; Q6IU50;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Crotonobetaine/carnitine--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01524, ECO:0000305};
DE EC=6.2.1.48 {ECO:0000255|HAMAP-Rule:MF_01524, ECO:0000269|PubMed:18266698};
DE AltName: Full=Betaine:CoA ligase {ECO:0000303|PubMed:18266698};
GN Name=caiC {ECO:0000255|HAMAP-Rule:MF_01524}; Synonyms=yaaM;
GN OrderedLocusNames=b0037, JW0036;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC STRAIN=O44:K74 / DSM 8828;
RX PubMed=7815937; DOI=10.1111/j.1365-2958.1994.tb00470.x;
RA Eichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.;
RT "Molecular characterization of the cai operon necessary for carnitine
RT metabolism in Escherichia coli.";
RL Mol. Microbiol. 13:775-786(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 285-459.
RC STRAIN=B;
RX PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
RA Lenski R.E., Winkworth C.L., Riley M.A.;
RT "Rates of DNA sequence evolution in experimental populations of Escherichia
RT coli during 20,000 generations.";
RL J. Mol. Evol. 56:498-508(2003).
RN [6]
RP PROBABLE FUNCTION.
RX PubMed=11749953; DOI=10.1016/s0014-5793(01)03178-7;
RA Heider J.;
RT "A new family of CoA-transferases.";
RL FEBS Lett. 509:345-349(2001).
RN [7]
RP PROBABLE FUNCTION.
RX PubMed=15518548; DOI=10.1021/bi048481c;
RA Stenmark P., Gurmu D., Nordlund P.;
RT "Crystal structure of CaiB, a type-III CoA transferase in carnitine
RT metabolism.";
RL Biochemistry 43:13996-14003(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=O44:K74 / DSM 8828;
RX PubMed=18266698; DOI=10.1111/j.1365-2672.2008.03740.x;
RA Bernal V., Arense P., Blatz V., Mandrand-Berthelot M.A., Canovas M.,
RA Iborra J.L.;
RT "Role of betaine:CoA ligase (CaiC) in the activation of betaines and the
RT transfer of coenzyme A in Escherichia coli.";
RL J. Appl. Microbiol. 105:42-50(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, ECO:0000269|PubMed:18266698}.
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 ECO:0000269|PubMed:18266698};
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 ECO:0000269|PubMed:18266698};
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 ECO:0000269|PubMed:18266698};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01524}.
CC -!- INTERACTION:
CC P31552; P0ACN4: allR; NbExp=3; IntAct=EBI-1112975, EBI-561736;
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01524, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB96606.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA52113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73904; CAA52113.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73148.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96606.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY625099; AAT42453.1; -; Genomic_DNA.
DR PIR; E64724; S40558.
DR RefSeq; NP_414579.4; NC_000913.3.
DR RefSeq; WP_001350478.1; NZ_LN832404.1.
DR AlphaFoldDB; P31552; -.
DR SMR; P31552; -.
DR BioGRID; 4261017; 531.
DR BioGRID; 849286; 2.
DR DIP; DIP-9243N; -.
DR IntAct; P31552; 5.
DR STRING; 511145.b0037; -.
DR TCDB; 4.C.1.1.6; the fatty acid group translocation (fat) family.
DR PaxDb; P31552; -.
DR PRIDE; P31552; -.
DR EnsemblBacteria; AAC73148; AAC73148; b0037.
DR EnsemblBacteria; BAB96606; BAB96606; BAB96606.
DR GeneID; 944886; -.
DR KEGG; ecj:JW0036; -.
DR KEGG; eco:b0037; -.
DR PATRIC; fig|1411691.4.peg.2246; -.
DR EchoBASE; EB1519; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_6; -.
DR InParanoid; P31552; -.
DR OMA; WLMQRAF; -.
DR PhylomeDB; P31552; -.
DR BioCyc; EcoCyc:CAIC-MON; -.
DR BioCyc; MetaCyc:CAIC-MON; -.
DR BRENDA; 6.2.1.48; 2026.
DR UniPathway; UPA00117; -.
DR PRO; PR:P31552; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:InterPro.
DR GO; GO:0051108; F:carnitine-CoA ligase activity; IDA:EcoCyc.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0051109; F:crotonobetaine-CoA ligase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Ligase; Reference proteome.
FT CHAIN 1..517
FT /note="Crotonobetaine/carnitine--CoA ligase"
FT /id="PRO_0000193065"
FT VARIANT 98
FT /note="C -> R (in strain: O44:K74)"
FT VARIANT 252..253
FT /note="RA -> PR (in strain: O44:K74)"
FT VARIANT 286
FT /note="Q -> R (in strain: O44:K74 and B)"
FT VARIANT 328
FT /note="I -> S (in strain: O44:K74)"
FT VARIANT 345
FT /note="V -> A (in strain: O44:K74 and B)"
FT VARIANT 359
FT /note="R -> C (in strain: B)"
FT VARIANT 374
FT /note="I -> V (in strain: O44:K74 and B)"
FT VARIANT 388
FT /note="Q -> K (in strain: O44:K74 and B)"
FT VARIANT 396
FT /note="A -> V (in strain: O44:K74)"
FT VARIANT 408
FT /note="R -> C (in strain: O44:K74)"
FT VARIANT 412
FT /note="D -> G (in strain: O44:K74 and B)"
FT VARIANT 442
FT /note="A -> T (in strain: O44:K74 and B)"
FT VARIANT 503
FT /note="L -> LDL (in strain: O44:K74)"
SQ SEQUENCE 517 AA; 58559 MW; C7A307D16200D8E9 CRC64;
MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLCEE SAWILQNSQA CLLVTSAQFY
PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
ATFVLVEKYS ARAFWGQVQK YRATVTECIP MMIRTLMVQP PSANDQQHRL REVMFYLNLS
EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFCYE AEIRDDHNRP
LPAGEIGEIC IKGIPGKTIF KEYFLNPQAT AKVLEADGWL HTGDTGYRDE EDFFYFVDRR
CNMIKRGGEN VSCVELENII AAHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
