(data stored in ACNUC7421 zone)

SWISSPROT: CAID_ECOL5

ID   CAID_ECOL5              Reviewed;         261 AA.
AC   Q0TLV3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   05-JUL-2017, entry version 71.
DE   RecName: Full=Carnitinyl-CoA dehydratase {ECO:0000255|HAMAP-Rule:MF_01051};
DE            EC=4.2.1.149 {ECO:0000255|HAMAP-Rule:MF_01051};
DE   AltName: Full=Crotonobetainyl-CoA hydratase {ECO:0000255|HAMAP-Rule:MF_01051};
GN   Name=caiD {ECO:0000255|HAMAP-Rule:MF_01051};
GN   OrderedLocusNames=ECP_0036;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA
CC       to crotonobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01051}.
CC   -!- CATALYTIC ACTIVITY: L-carnitinyl-CoA = (E)-4-
CC       (trimethylammonio)but-2-enoyl-CoA + H(2)O. {ECO:0000255|HAMAP-
CC       Rule:MF_01051}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01051}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01051}.
DR   EMBL; CP000247; ABG68078.1; -; Genomic_DNA.
DR   RefSeq; WP_000004399.1; NC_008253.1.
DR   ProteinModelPortal; Q0TLV3; -.
DR   SMR; Q0TLV3; -.
DR   EnsemblBacteria; ABG68078; ABG68078; ECP_0036.
DR   KEGG; ecp:ECP_0036; -.
DR   eggNOG; ENOG4106YT9; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; KGRAMEM; -.
DR   UniPathway; UPA00117; -.
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; Q0TLV3.
DR   SWISS-2DPAGE; Q0TLV3.
KW   Lyase.
FT   CHAIN         1    261       Carnitinyl-CoA dehydratase.
FT                                /FTId=PRO_1000064341.
FT   SITE        111    111       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01051}.
FT   SITE        131    131       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01051}.
SQ   SEQUENCE   261 AA;  28176 MW;  D2BC39DD3E6983B6 CRC64;
     MSESLHLTRN GSILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPQLRVA IITGAGEKFF
     SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FNLDKPVIAA VNGYAFGGGF ELALAADFIV
     CADNASFALP EAKLGIVPDS GGVLRLPKIL PPAIVNEMVM TGRRMGAEEA LRWGVVNRVV
     SQAELMDNAR ELAQQLVNSA PLAIAALKEI YRTTSEMPVE EAYRYIRSGV LKHYPSVLHS
     EDAIEGPLAF AEKRDPVWKG R
//

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