(data stored in ACNUC7421 zone)

SWISSPROT: Q1RGG2_ECOUT

ID   Q1RGG2_ECOUT            Unreviewed;       297 AA.
AC   Q1RGG2;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   07-JUN-2017, entry version 71.
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:ABE05552.1};
GN   OrderedLocusNames=UTI89_C0042 {ECO:0000313|EMBL:ABE05552.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE05552.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE05552.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE05552.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q1RGG2; -.
DR   EnsemblBacteria; ABE05552; ABE05552; UTI89_C0042.
DR   KEGG; eci:UTI89_C0042; -.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; KGRAMEM; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001952; 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; Q1RGG2.
DR   SWISS-2DPAGE; Q1RGG2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001952};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01051, ECO:0000313|EMBL:ABE05552.1}.
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;  32285 MW;  9F568751F97EB885 CRC64;
     MKRQGTTLSA NNHALKQYAF FAGMLSSLKK QKWRKGMSES LHLTRNGSIL EITLDRPKAN
     AIDAKTSFEM GEVFLNFRDD PQLRVAIITG AGEKFFSAGW DLKAAAEGEA PDADFGPGGF
     AGLTEIFNLD KPVIAAVNGY AFGGGFELAL AADFIVCADN ASFALPEAKL GIVPDSGGVL
     RLPKILPPAI VNEMVMTGRR MGAEEALRWG VVNRVVSQAE LMDNARELAQ QLVNSAPLAI
     AALKEIYRTT SEMPVEEAYR YIRSGVLKHY PSVLHSEDAI EGPLAFAEKR DPVWKGR
//

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