(data stored in ACNUC7421 zone)

SWISSPROT: D2TGM2_CITRI

ID   D2TGM2_CITRI            Unreviewed;       261 AA.
AC   D2TGM2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   07-JUN-2017, entry version 48.
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:CBG86819.1};
GN   OrderedLocusNames=ROD_00381 {ECO:0000313|EMBL:CBG86819.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype
OS   4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG86819.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG86819.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG86819.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M.,
RA   Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A.,
RA   Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G.,
RA   Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent
RT   evolution with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG86819.1; -; Genomic_DNA.
DR   RefSeq; WP_012904424.1; NC_013716.1.
DR   ProteinModelPortal; D2TGM2; -.
DR   STRING; 637910.ROD_00381; -.
DR   EnsemblBacteria; CBG86819; CBG86819; ROD_00381.
DR   KEGG; cro:ROD_00381; -.
DR   eggNOG; ENOG4106YT9; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   HOGENOM; HOG000027939; -.
DR   KO; K08299; -.
DR   OMA; KGRAMEM; -.
DR   OrthoDB; POG091H01K6; -.
DR   UniPathway; UPA00117; -.
DR   Proteomes; UP000001889; 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; D2TGM2.
DR   SWISS-2DPAGE; D2TGM2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001889};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01051, ECO:0000313|EMBL:CBG86819.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001889}.
FT   SITE        111    111       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01051}.
FT   SITE        131    131       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01051}.
SQ   SEQUENCE   261 AA;  28029 MW;  C2DFC11A96D3BFD4 CRC64;
     MSESLHLTRN GAVLEIILDR PKANAIDART SFQMGEVFLN FRDDPELRVA IVTGAGEKFF
     SAGWDLKAAA EGEAPDADFG PGGFAGLTEC FDLDKPVIAA VNGYAFGGGF ELALAADFIV
     CADHASFALP EARLGIVPDS GGVLRLPKRL PPVIANEMVM TGRRMSAGEA LRWGIVNRVV
     SQQALMDSAR ELAQQLVSSA PLAIAALKEI YRATGEMSVE EGYRCLRSGA LKHYPAVLHS
     EDALEGPRAF AEKRDPVWKG R
//

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