CAIB_ECOLI
ID CAIB_ECOLI Reviewed; 405 AA.
AC P31572;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 174.
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, ECO:0000269|PubMed:11551212};
DE AltName: Full=Crotonobetainyl-CoA:carnitine CoA-transferase {ECO:0000255|HAMAP-Rule:MF_01050};
GN Name=caiB {ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000303|PubMed:8188598};
GN Synonyms=yaaN; OrderedLocusNames=b0038, JW0037;
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 PROTEIN SEQUENCE OF 1-19.
RC STRAIN=O44:K74;
RX PubMed=8188598; DOI=10.1128/jb.176.10.2970-2975.1994;
RA Eichler K., Schunck W.-H., Kleber H.-P., Mandrand-Berthelot M.-A.;
RT "Cloning, nucleotide sequence, and expression of the Escherichia coli gene
RT encoding carnitine dehydratase.";
RL J. Bacteriol. 176:2970-2975(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O44:K74;
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=O44:K74;
RX PubMed=11551212; DOI=10.1021/bi0108812;
RA Elssner T., Engemann C., Baumgart K., Kleber H.-P.;
RT "Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA
RT hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-
RT carnitine by Escherichia coli.";
RL Biochemistry 40:11140-11148(2001).
RN [7]
RP ENZYME ACTIVITY UNDER AEROBIOSIS.
RC STRAIN=ATCC 25922 / DSM 1103 / NCIB 12210, and O44:K74;
RX PubMed=10339822; DOI=10.1111/j.1574-6968.1999.tb13582.x;
RA Elssner T., Preusser A., Wagner U., Kleber H.-P.;
RT "Metabolism of L(-)-carnitine by Enterobacteriaceae under aerobic
RT conditions.";
RL FEMS Microbiol. Lett. 174:295-301(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH COENZYME A, AND
RP ACTIVE SITE.
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).
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, ECO:0000269|PubMed:11551212}.
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 ECO:0000269|PubMed:11551212};
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, ECO:0000269|PubMed:11551212};
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000269|PubMed:11551212}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01050,
CC ECO:0000269|PubMed:15518548}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01050}.
CC -!- INDUCTION: By L-carnitine or crotonobetaine.
CC -!- MISCELLANEOUS: Some strains of E.coli, such as ATCC 25922, can
CC metabolize carnitine under aerobiosis. {ECO:0000305|PubMed:10339822}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an L-carnitine dehydratase.
CC {ECO:0000305|PubMed:8188598}.
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DR EMBL; X67748; CAA47971.1; -; Genomic_DNA.
DR EMBL; X73904; CAA52112.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73149.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96607.1; -; Genomic_DNA.
DR PIR; S40559; S40559.
DR RefSeq; NP_414580.1; NC_000913.3.
DR RefSeq; WP_000349936.1; NZ_LN832404.1.
DR PDB; 1XA3; X-ray; 1.85 A; A/B=2-405.
DR PDB; 1XA4; X-ray; 1.90 A; A/B=2-405.
DR PDB; 1XK6; X-ray; 1.85 A; A/B/C/D=1-405.
DR PDB; 1XK7; X-ray; 1.60 A; A/B/C=1-405.
DR PDB; 1XVT; X-ray; 2.30 A; A=1-405.
DR PDB; 1XVU; X-ray; 2.40 A; A=1-405.
DR PDB; 1XVV; X-ray; 2.40 A; A=1-405.
DR PDBsum; 1XA3; -.
DR PDBsum; 1XA4; -.
DR PDBsum; 1XK6; -.
DR PDBsum; 1XK7; -.
DR PDBsum; 1XVT; -.
DR PDBsum; 1XVU; -.
DR PDBsum; 1XVV; -.
DR AlphaFoldDB; P31572; -.
DR SMR; P31572; -.
DR BioGRID; 4261584; 5.
DR BioGRID; 853245; 1.
DR IntAct; P31572; 12.
DR STRING; 511145.b0038; -.
DR DrugBank; DB02516; (R)-carnitinyl-CoA betaine.
DR DrugBank; DB01992; Coenzyme A.
DR PaxDb; P31572; -.
DR PRIDE; P31572; -.
DR EnsemblBacteria; AAC73149; AAC73149; b0038.
DR EnsemblBacteria; BAB96607; BAB96607; BAB96607.
DR GeneID; 948997; -.
DR KEGG; ecj:JW0037; -.
DR KEGG; eco:b0038; -.
DR PATRIC; fig|1411691.4.peg.2245; -.
DR EchoBASE; EB1520; -.
DR eggNOG; COG1804; Bacteria.
DR HOGENOM; CLU_033975_2_0_6; -.
DR InParanoid; P31572; -.
DR OMA; HRPGFGT; -.
DR PhylomeDB; P31572; -.
DR BioCyc; EcoCyc:CARNDEHYDRA-MON; -.
DR BioCyc; MetaCyc:CARNDEHYDRA-MON; -.
DR BRENDA; 2.8.3.21; 2026.
DR UniPathway; UPA00117; -.
DR EvolutionaryTrace; P31572; -.
DR PRO; PR:P31572; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008735; F:carnitine dehydratase activity; EXP:EcoliWiki.
DR GO; GO:0008410; F:CoA-transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042413; P:carnitine catabolic process; EXP:EcoliWiki.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Transferase.
FT CHAIN 1..405
FT /note="L-carnitine CoA-transferase"
FT /id="PRO_0000194708"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050,
FT ECO:0000305|PubMed:15518548"
FT BINDING 97
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050,
FT ECO:0000269|PubMed:15518548"
FT BINDING 104
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01050,
FT ECO:0000269|PubMed:15518548"
FT VARIANT 187
FT /note="V -> A (in strain: O44:K74)"
FT VARIANT 302
FT /note="T -> A (in strain: O44:K74)"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:1XK7"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1XA3"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1XK7"
FT TURN 132..136
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1XK7"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 167..190
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:1XK7"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 289..301
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1XK7"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 378..384
FT /evidence="ECO:0007829|PDB:1XK7"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:1XK7"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:1XK7"
SQ SEQUENCE 405 AA; 45127 MW; 75583684B4B5A2DE 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
ATHTIAEVKE RFAELNIACA KVLTVPELES NPQYVARESI TQWQTMDGRT CKGPNIMPKF
KNNPGQIWRG MPSHGMDTAA ILKNIGYSEN DIQELVSKGL AKVED
