(data stored in ACNUC7421 zone)

SWISSPROT: CAID_ECO57

ID   CAID_ECO57              Reviewed;         261 AA.
AC   Q8XA35;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   07-JUN-2017, entry version 93.
DE   RecName: Full=Carnitinyl-CoA dehydratase;
DE            EC=4.2.1.149;
DE   AltName: Full=Crotonobetainyl-CoA hydratase;
GN   Name=caiD; OrderedLocusNames=Z0042, ECs0039;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA
CC       to crotonobetainyl-CoA. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: L-carnitinyl-CoA = (E)-4-
CC       (trimethylammonio)but-2-enoyl-CoA + H(2)O.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG54339.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB33462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE005174; AAG54339.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB33462.1; ALT_INIT; Genomic_DNA.
DR   PIR; G85484; G85484.
DR   PIR; G90633; G90633.
DR   RefSeq; NP_308066.2; NC_002695.1.
DR   RefSeq; WP_001303785.1; NZ_LPWC02000002.1.
DR   ProteinModelPortal; Q8XA35; -.
DR   SMR; Q8XA35; -.
DR   STRING; 155864.Z0042; -.
DR   EnsemblBacteria; AAG54339; AAG54339; Z0042.
DR   EnsemblBacteria; BAB33462; BAB33462; BAB33462.
DR   GeneID; 913435; -.
DR   KEGG; ece:Z0042; -.
DR   KEGG; ecs:ECs0039; -.
DR   PATRIC; fig|386585.9.peg.136; -.
DR   eggNOG; ENOG4106YT9; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   HAMAP; MF_01051; CaiD; 1.
DR   InterPro; IPR022852; Carnitinyl_CoA_dehydratase.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR014748; Crontonase_C.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XA35.
DR   SWISS-2DPAGE; Q8XA35.
KW   Complete proteome; Lyase.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    261       Carnitinyl-CoA dehydratase.
FT                                /FTId=PRO_0000109350.
FT   SITE        111    111       Important for catalytic activity.
FT                                {ECO:0000250}.
FT   SITE        131    131       Important for catalytic activity.
FT                                {ECO:0000250}.
SQ   SEQUENCE   261 AA;  28137 MW;  5F96ACC3D1683ECF CRC64;
     MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA IITGAGEKFF
     SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA VNGYAFGGGF ELALAADFIV
     CADNASFALP EAKLGIVPDS GGVLRLPKIL PPAIVNEMVM TGRRMGAEEA LRWGIVNRVV
     SQAELMDNAR ELAQQLVNSA PLAIAALKEI YRTTSEMPVE ESYSYIRSGV LKHYPSVLHS
     EDAIEGPLAF AEKRDPVWKG R
//

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