CAIC_SHIFL
ID CAIC_SHIFL Reviewed; 517 AA.
AC Q83MG9; Q7C3C0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 105.
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=SF0034, S0036;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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=AAN41700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP15581.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN41700.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP15581.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_705993.1; NC_004337.2.
DR RefSeq; WP_005053636.1; NZ_WPGW01000005.1.
DR AlphaFoldDB; Q83MG9; -.
DR SMR; Q83MG9; -.
DR STRING; 198214.SF0034; -.
DR EnsemblBacteria; AAN41700; AAN41700; SF0034.
DR EnsemblBacteria; AAP15581; AAP15581; S0036.
DR GeneID; 1024583; -.
DR GeneID; 58390360; -.
DR KEGG; sfl:SF0034; -.
DR KEGG; sfx:S0036; -.
DR PATRIC; fig|198214.7.peg.40; -.
DR HOGENOM; CLU_000022_59_0_6; -.
DR OrthoDB; 377638at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000193073"
SQ SEQUENCE 517 AA; 58661 MW; A28EBFF776C86956 CRC64;
MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
KGNKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLREE SEWILQNSQA CLLVTSAQFY
PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYMTV MPAFHIDCQC TAAMAAFSAG
ATFVLVEKYS ARAFWGQAQK YRATITECIP MMIRTLMVQP PSANDRQHRL REVMFYLNLS
EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPSDKRRWP SIGRAGFCYE AEIRDDHNRP
LPAGEIGEIC IKGVPGKTIF KEYFLNPKAT AKVLEADGWL HTGDTGYRDE EGFFYFVDRR
CNMIKRGGEN VSCVELENII ATHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
