CAIB_SHIFL
ID CAIB_SHIFL Reviewed; 405 AA.
AC P59394;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=L-carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
DE EC=2.8.3.21 {ECO:0000255|HAMAP-Rule:MF_01050};
DE AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
GN Name=caiB {ECO:0000255|HAMAP-Rule:MF_01050};
GN OrderedLocusNames=SF0035, S0037;
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 reversible transfer of the CoA moiety from
CC gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA
CC and gamma-butyrobetaine. Is also able to catalyze the reversible
CC transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-
CC carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + crotonobetainyl-CoA = (R)-carnitinyl-CoA +
CC crotonobetaine; Xref=Rhea:RHEA:28526, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:17237, ChEBI:CHEBI:60932, ChEBI:CHEBI:60933; EC=2.8.3.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + gamma-butyrobetainyl-CoA = (R)-carnitinyl-CoA
CC + 4-(trimethylamino)butanoate; Xref=Rhea:RHEA:28418,
CC ChEBI:CHEBI:16244, ChEBI:CHEBI:16347, ChEBI:CHEBI:60932,
CC ChEBI:CHEBI:61513; EC=2.8.3.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01050};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01050}.
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DR EMBL; AE005674; AAN41701.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP15582.1; -; Genomic_DNA.
DR RefSeq; NP_705994.1; NC_004337.2.
DR RefSeq; WP_000349932.1; NZ_WPGW01000005.1.
DR AlphaFoldDB; P59394; -.
DR SMR; P59394; -.
DR STRING; 198214.SF0035; -.
DR EnsemblBacteria; AAN41701; AAN41701; SF0035.
DR EnsemblBacteria; AAP15582; AAP15582; S0037.
DR GeneID; 1024543; -.
DR GeneID; 58390359; -.
DR KEGG; sfl:SF0035; -.
DR KEGG; sfx:S0037; -.
DR PATRIC; fig|198214.7.peg.41; -.
DR HOGENOM; CLU_033975_2_0_6; -.
DR OMA; HRPGFGT; -.
DR OrthoDB; 969868at2; -.
DR UniPathway; UPA00117; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008410; F:CoA-transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR HAMAP; MF_01050; CaiB; 1.
DR InterPro; IPR023452; CoA-Trfase_CaiB.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..405
FT /note="L-carnitine CoA-transferase"
FT /id="PRO_0000194714"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT BINDING 97
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
FT BINDING 104
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050"
SQ SEQUENCE 405 AA; 45097 MW; 94583684B4A4B3C3 CRC64;
MDHLPMPKFG PLAGLRVVFS GIEIAGPFAG QMFAEWGAEV IWIENVAWAD TIRVQPNYPQ
LSRRNLHALS LNIFKDEGRE AFLKLMETTD IFIEASKGPA FARRGITDEV LWQHNPKLVI
AHLSGFGQYG TEEYTNLPAY NTIAQAFSGY LIQNGDVDQP MPAFPYTADY FSGLTATTAA
LAALHKVRET GKGESIDIAM YEVMLRMGQY FMMDYFNGGE MCPRMSKGKD PYYAGCGLYK
CADGYIVMEL VGITQIEECF KDIGLAHLLG TPEIPEGTQL IHRIECPYGP LVEEKLDAWL
AAHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
