(data stored in ACNUC7421 zone)

SWISSPROT: C8UGQ5_ECO1A

ID   C8UGQ5_ECO1A            Unreviewed;       297 AA.
AC   C8UGQ5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   07-JUN-2017, entry version 46.
DE   RecName: Full=Carnitinyl-CoA dehydratase {ECO:0000256|HAMAP-Rule:MF_01051};
DE            EC=4.2.1.149 {ECO:0000256|HAMAP-Rule:MF_01051};
DE   AltName: Full=Crotonobetainyl-CoA hydratase {ECO:0000256|HAMAP-Rule:MF_01051};
GN   Name=caiD {ECO:0000256|HAMAP-Rule:MF_01051,
GN   ECO:0000313|EMBL:BAI34038.1};
GN   OrderedLocusNames=ECO111_0037 {ECO:0000313|EMBL:BAI34038.1};
OS   Escherichia coli O111:H- (strain 11128 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585396 {ECO:0000313|EMBL:BAI34038.1, ECO:0000313|Proteomes:UP000001614};
RN   [1] {ECO:0000313|EMBL:BAI34038.1, ECO:0000313|Proteomes:UP000001614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11128 / EHEC {ECO:0000313|Proteomes:UP000001614};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA
CC       to crotonobetainyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01051}.
CC   -!- CATALYTIC ACTIVITY: L-carnitinyl-CoA = (E)-4-
CC       (trimethylammonio)but-2-enoyl-CoA + H(2)O. {ECO:0000256|HAMAP-
CC       Rule:MF_01051}.
CC   -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_01051}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01051, ECO:0000256|RuleBase:RU003707}.
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DR   EMBL; AP010960; BAI34038.1; -; Genomic_DNA.
DR   ProteinModelPortal; C8UGQ5; -.
DR   EnsemblBacteria; BAI34038; BAI34038; ECO111_0037.
DR   KEGG; eoi:ECO111_0037; -.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; KGRAMEM; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001614; Chromosome.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-HAMAP.
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; C8UGQ5.
DR   SWISS-2DPAGE; C8UGQ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001614};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01051}.
FT   SITE        147    147       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01051}.
FT   SITE        167    167       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01051}.
SQ   SEQUENCE   297 AA;  32265 MW;  3F1C3EDC4C1B0CF1 CRC64;
     MKQQGTTLPA NNHAIKQYAF FAGMLSSLKK QKWRKGMSES LHLTRNGSIL EITLDRPKAN
     AIDAKTSFEM GEVFLNFRDD PQLRVAIITG AGEKFFSAGW DLKAAAEGEA PDADFGPGGF
     AGLTEIFNLD KPVIAAVNGY AFGGGFELAL AADFIVCADN ASFALPEAKL GIVPDSGGVL
     RLPKILPPAI VNEMVMTGRR MGAEEALRWG IVNRVVSQAE LMDNARELAQ QLVNSAPLAI
     AALKEIFRTT SEMPVEEAYR YIRSGVLKHY PSVLHSEDAI EGPLAFAEKR DPVWKGR
//

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