(data stored in ACNUC7421 zone)

SWISSPROT: C8U1B0_ECO10

ID   C8U1B0_ECO10            Unreviewed;       297 AA.
AC   C8U1B0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
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:BAI28918.1};
GN   OrderedLocusNames=ECO103_0038 {ECO:0000313|EMBL:BAI28918.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28918.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28918.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
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:
CC       Reaction=(R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O;
CC         Xref=Rhea:RHEA:28338, ChEBI:CHEBI:15377, ChEBI:CHEBI:60932,
CC         ChEBI:CHEBI:60933; EC=4.2.1.149; Evidence={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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010958; BAI28918.1; -; Genomic_DNA.
DR   EnsemblBacteria; BAI28918; BAI28918; ECO103_0038.
DR   KEGG; eoh:ECO103_0038; -.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; AMEMIMT; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
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_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
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; C8U1B0.
DR   SWISS-2DPAGE; C8U1B0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  32297 MW;  22BC9E6A8ACAC8B4 CRC64;
     MKQQGTTLPA NNHAIKQYAF FAGMLSSLKK QKWRKGMSES LHLTRNGSIL EITLDRPKAN
     AIDAKTSFEM GEVFLNFRDD PQLRVAIITG AGEKFFSAGW DLKAAAEGEA PDADFGPGGF
     AGLTEIFNLD KPVIAAVNGY AFGGGFELAL AADFIVCADN ASFALPEAKL GIVPDSGGVL
     RLPKILPPAI VNEMVMTGRR MGTEEALRWG IVNRVVSQAE LMDNARELAQ QLVNSAPLAI
     AALKEIYRTT SEMPVEEAYR YIRSGVLKHY PSVLHSEDAV EGPLAFAEKR DPVWKGR
//

If you have problems or comments...

PBIL Back to PBIL home page