(data stored in SCRATCH zone)

SWISSPROT: ECHM_RAT

ID   ECHM_RAT                Reviewed;         290 AA.
AC   P14604;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   30-AUG-2017, entry version 153.
DE   RecName: Full=Enoyl-CoA hydratase, mitochondrial;
DE            EC=4.2.1.17 {ECO:0000250|UniProtKB:P30084};
DE   AltName: Full=Enoyl-CoA hydratase 1;
DE   AltName: Full=Short-chain enoyl-CoA hydratase;
DE            Short=SCEH;
DE   Flags: Precursor;
GN   Name=Echs1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-39 AND 80-94.
RC   TISSUE=Liver;
RX   PubMed=2806264; DOI=10.1111/j.1432-1033.1989.tb15083.x;
RA   Minami-Ishii N., Taketani S., Osumi T., Hashimoto T.;
RT   "Molecular cloning and sequence analysis of the cDNA for rat
RT   mitochondrial enoyl-CoA hydratase. Structural and evolutionary
RT   relationships linked to the bifunctional enzyme of the peroxisomal
RT   beta-oxidation system.";
RL   Eur. J. Biochem. 185:73-78(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   MUTAGENESIS OF GLU-164.
RX   PubMed=7883013; DOI=10.1111/j.1432-1033.1995.tb20230.x;
RA   Mueller-Newen G., Janssen U., Stoffel W.;
RT   "Enoyl-CoA hydratase and isomerase form a superfamily with a common
RT   active-site glutamate residue.";
RL   Eur. J. Biochem. 228:68-73(1995).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH OCTANOYL
RP   COENZYME A, AND SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=8895557;
RA   Engel C.K., Mathieu M., Zeelen J.P., Hiltunen J.K., Wierenga R.K.;
RT   "Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5-A
RT   resolution: a spiral fold defines the CoA-binding pocket.";
RL   EMBO J. 15:5135-5145(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ACETOACETYL
RP   COENZYME A, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9480773; DOI=10.1006/jmbi.1997.1491;
RA   Engel C.K., Kiema T.R., Hiltunen J.K., Wierenga R.K.;
RT   "The crystal structure of enoyl-CoA hydratase complexed with octanoyl-
RT   CoA reveals the structural adaptations required for binding of a long
RT   chain fatty acid-CoA molecule.";
RL   J. Mol. Biol. 275:847-859(1998).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-290 IN COMPLEX WITH
RP   4-N,N-DIMETHYLAMINOCINNAMOYL COENZYME A, ENZYME MECHANISM, AND
RP   SUBUNIT.
RX   PubMed=11851409; DOI=10.1021/bi015844p;
RA   Bahnson B.J., Anderson V.E., Petsko G.A.;
RT   "Structural mechanism of enoyl-CoA hydratase: three atoms from a
RT   single water are added in either an E1cb stepwise or concerted
RT   fashion.";
RL   Biochemistry 41:2621-2629(2002).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-290 IN COMPLEX WITH
RP   HEXADIENOL COENZYME A, AND MUTAGENESIS OF GLU-144.
RX   PubMed=12445775; DOI=10.1016/S1074-5521(02)00263-6;
RA   Bell A.F., Feng Y., Hofstein H.A., Parikh S., Wu J., Rudolph M.J.,
RA   Kisker C., Whitty A., Tonge P.J.;
RT   "Stereoselectivity of enoyl-CoA hydratase results from preferential
RT   activation of one of two bound substrate conformers.";
RL   Chem. Biol. 9:1247-1255(2002).
CC   -!- FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at
CC       least C16 are processed, although with decreasing catalytic rate.
CC       Has high substrate specificity for crotonyl-CoA and moderate
CC       specificity for acryloyl-CoA, 3-methylcrotonyl-CoA and
CC       methacrylyl-CoA. It is noteworthy that binds tiglyl-CoA, but
CC       hydrates only a small amount of this substrate.
CC       {ECO:0000250|UniProtKB:P30084}.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O. {ECO:0000250|UniProtKB:P30084}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:P30084}.
CC   -!- SUBUNIT: Homohexamer; dimer of trimers.
CC       {ECO:0000269|PubMed:11851409, ECO:0000269|PubMed:12445775,
CC       ECO:0000269|PubMed:8895557, ECO:0000269|PubMed:9480773}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:9480773}.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC       {ECO:0000269|PubMed:9480773}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
DR   EMBL; X15958; CAA34080.1; -; mRNA.
DR   EMBL; BC064655; AAH64655.1; -; mRNA.
DR   PIR; S06477; S06477.
DR   RefSeq; NP_511178.1; NM_078623.2.
DR   RefSeq; XP_003748934.1; XM_003748886.3.
DR   UniGene; Rn.6847; -.
DR   PDB; 1DUB; X-ray; 2.50 A; A/B/C/D/E/F=30-290.
DR   PDB; 1EY3; X-ray; 2.30 A; A/B/C/D/E/F=33-290.
DR   PDB; 1MJ3; X-ray; 2.10 A; A/B/C/D/E/F=31-290.
DR   PDB; 2DUB; X-ray; 2.40 A; A/B/C/D/E/F=30-290.
DR   PDBsum; 1DUB; -.
DR   PDBsum; 1EY3; -.
DR   PDBsum; 1MJ3; -.
DR   PDBsum; 2DUB; -.
DR   ProteinModelPortal; P14604; -.
DR   SMR; P14604; -.
DR   IntAct; P14604; 1.
DR   STRING; 10116.ENSRNOP00000066388; -.
DR   ChEMBL; CHEMBL3153; -.
DR   SwissLipids; SLP:000001128; -.
DR   iPTMnet; P14604; -.
DR   PhosphoSitePlus; P14604; -.
DR   PaxDb; P14604; -.
DR   PRIDE; P14604; -.
DR   Ensembl; ENSRNOT00000025446; ENSRNOP00000025446; ENSRNOG00000018522.
DR   Ensembl; ENSRNOT00000071574; ENSRNOP00000066388; ENSRNOG00000047565.
DR   GeneID; 100911186; -.
DR   GeneID; 140547; -.
DR   KEGG; rno:100911186; -.
DR   KEGG; rno:140547; -.
DR   UCSC; RGD:69330; rat.
DR   CTD; 1892; -.
DR   RGD; 69330; Echs1.
DR   eggNOG; KOG1680; Eukaryota.
DR   eggNOG; COG1024; LUCA.
DR   GeneTree; ENSGT00890000139344; -.
DR   HOGENOM; HOG000027939; -.
DR   HOVERGEN; HBG010157; -.
DR   InParanoid; P14604; -.
DR   KO; K07511; -.
DR   OMA; IFKQTDA; -.
DR   OrthoDB; EOG091G0MVQ; -.
DR   PhylomeDB; P14604; -.
DR   TreeFam; TF314497; -.
DR   BRENDA; 4.2.1.17; 5301.
DR   Reactome; R-RNO-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR   Reactome; R-RNO-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR   Reactome; R-RNO-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR   Reactome; R-RNO-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR   Reactome; R-RNO-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR   UniPathway; UPA00659; -.
DR   EvolutionaryTrace; P14604; -.
DR   PRO; PR:P14604; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018522; -.
DR   Genevisible; P14604; RN.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:RGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:RGD.
DR   Gene3D; 1.10.12.10; -; 1.
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   1: Evidence at protein level;
DR   PRODOM; P14604.
DR   SWISS-2DPAGE; P14604.
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; Fatty acid metabolism; Lipid metabolism;
KW   Lyase; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion.
FT                                {ECO:0000269|PubMed:2806264}.
FT   CHAIN        30    290       Enoyl-CoA hydratase, mitochondrial.
FT                                /FTId=PRO_0000007414.
FT   REGION       98    101       Substrate binding.
FT   BINDING     141    141       Substrate; via amide nitrogen.
FT   SITE        164    164       Important for catalytic activity.
FT   MOD_RES     101    101       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8BH95}.
FT   MOD_RES     101    101       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8BH95}.
FT   MOD_RES     115    115       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8BH95}.
FT   MOD_RES     115    115       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8BH95}.
FT   MOD_RES     204    204       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8BH95}.
FT   MOD_RES     211    211       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8BH95}.
FT   MUTAGEN     144    144       E->D: Reduces activity 50-fold.
FT                                {ECO:0000269|PubMed:12445775}.
FT   MUTAGEN     144    144       E->Q: Reduces activity 3300-fold.
FT                                {ECO:0000269|PubMed:12445775}.
FT   MUTAGEN     164    164       E->D: Reduces activity 1250-fold.
FT                                {ECO:0000269|PubMed:7883013}.
FT   MUTAGEN     164    164       E->Q: Reduces activity 330000-fold.
FT                                {ECO:0000269|PubMed:7883013}.
FT   STRAND       34     42       {ECO:0000244|PDB:1MJ3}.
FT   HELIX        43     45       {ECO:0000244|PDB:1MJ3}.
FT   STRAND       47     52       {ECO:0000244|PDB:1MJ3}.
FT   HELIX        55     57       {ECO:0000244|PDB:1MJ3}.
FT   HELIX        63     78       {ECO:0000244|PDB:1MJ3}.
FT   STRAND       84     88       {ECO:0000244|PDB:1MJ3}.
FT   STRAND       91     95       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       100    103       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       108    113       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       119    125       {ECO:0000244|PDB:1MJ3}.
FT   STRAND      130    134       {ECO:0000244|PDB:1MJ3}.
FT   STRAND      136    139       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       141    148       {ECO:0000244|PDB:1MJ3}.
FT   STRAND      149    155       {ECO:0000244|PDB:1MJ3}.
FT   STRAND      159    161       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       163    167       {ECO:0000244|PDB:1MJ3}.
FT   TURN        175    177       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       178    183       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       185    194       {ECO:0000244|PDB:1MJ3}.
FT   STRAND      197    199       {ECO:0000244|PDB:2DUB}.
FT   HELIX       200    205       {ECO:0000244|PDB:1MJ3}.
FT   STRAND      210    213       {ECO:0000244|PDB:1MJ3}.
FT   TURN        215    217       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       218    231       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       234    245       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       246    248       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       252    265       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       266    268       {ECO:0000244|PDB:1MJ3}.
FT   HELIX       270    280       {ECO:0000244|PDB:1MJ3}.
SQ   SEQUENCE   290 AA;  31516 MW;  1E528590961D0CC0 CRC64;
     MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA
     LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI KEMQNRTFQD CYSGKFLSHW
     DHITRIKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT
     RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA
     KESVNAAFEM TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH
//

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