(data stored in ACNUC7421 zone)

SWISSPROT: CAID_CITK8

ID   CAID_CITK8              Reviewed;         261 AA.
AC   A8ALR7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   07-JUN-2017, entry version 60.
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=CKO_03347;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV14430.1; -; Genomic_DNA.
DR   RefSeq; WP_012134133.1; NC_009792.1.
DR   ProteinModelPortal; A8ALR7; -.
DR   SMR; A8ALR7; -.
DR   STRING; 290338.CKO_03347; -.
DR   EnsemblBacteria; ABV14430; ABV14430; CKO_03347.
DR   KEGG; cko:CKO_03347; -.
DR   eggNOG; ENOG4105E39; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; KGRAMEM; -.
DR   OrthoDB; POG091H01K6; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000008148; Chromosome.
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; A8ALR7.
DR   SWISS-2DPAGE; A8ALR7.
KW   Complete proteome; Lyase; Reference proteome.
FT   CHAIN         1    261       Carnitinyl-CoA dehydratase.
FT                                /FTId=PRO_1000064340.
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;  28232 MW;  503DF8B6644036CF CRC64;
     MSESLHFTRH GPILEITLDR PKANAIDAKT SFEMGEVFLN FRDDPELRVA IITGGGEKFF
     SAGWDLKAAA EGEAPDADFG PGGFAGLTEI FDLDKPVIAA VNGYAFGGGF ELALAADFIV
     CADNASFALP EAKLGIVPDS GGVLRLPKLL PPAIVNEMLM TGRRMDAEEA LRWGIVNRVV
     SQQALMDSAR ELAQQLVNSA PLAIAALKEI YRATSEMPVE EGYRYIRSGA LKHYPSVLHS
     EDAIEGPQAF AEKRDPVWKG R
//

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