(data stored in ACNUC7421 zone)

SWISSPROT: B7UI82_ECO27

ID   B7UI82_ECO27            Unreviewed;       297 AA.
AC   B7UI82;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-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:CAS07585.1};
GN   OrderedLocusNames=E2348C_0037 {ECO:0000313|EMBL:CAS07585.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07585.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07585.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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}.
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DR   EMBL; FM180568; CAS07585.1; -; Genomic_DNA.
DR   EnsemblBacteria; CAS07585; CAS07585; E2348C_0037.
DR   KEGG; ecg:E2348C_0037; -.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; AMEMIMT; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008205; 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; B7UI82.
DR   SWISS-2DPAGE; B7UI82.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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;  32237 MW;  EE20C53568751D7E CRC64;
     MKRQGTTLPA NNHALKQYAF FAGMLSSLKK QKWRKGMSES LHLTRNGSIL EITLDRPKAN
     AIDAKTSFEM GEVFLNFRDD PQLRVAIITG AGEKFFSAGW DLKAAAEGEA PDADFGPGGF
     AGLTEIFNLD KPVIAAVNGY AFGGGFELAL AADFIVCADN ASFALPEAKL GIVPDSGGVL
     RLPKILPPAI VNEMVMTGRR MGAEEALRWG VVNRVVSQAE LMDNARELAQ QLVNSAPLAI
     AALKEIYRTT SAMPVEEAYR YIRSGVLKHY PSVLHSEDAI EGPLAFAEKR DPVWKGR
//

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