ECHM_MOUSE
ID ECHM_MOUSE Reviewed; 290 AA.
AC Q8BH95; Q3TJK2; Q6GQS2; Q6PEN1; Q99LX7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Enoyl-CoA hydratase, mitochondrial {ECO:0000305};
DE Short=mECH;
DE Short=mECH1;
DE EC=4.2.1.17 {ECO:0000250|UniProtKB:P30084};
DE EC=5.3.3.8 {ECO:0000250|UniProtKB:P14604};
DE AltName: Full=Enoyl-CoA hydratase 1;
DE Short=ECHS1;
DE AltName: Full=Short-chain enoyl-CoA hydratase;
DE Short=SCEH;
DE Flags: Precursor;
GN Name=Echs1 {ECO:0000312|MGI:MGI:2136460};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 116-125; 158-178 AND 274-282, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-115; LYS-204 AND
RP LYS-217, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101; LYS-115; LYS-211 AND
RP LYS-217, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-
CC CoA) to the corresponding (3S)-3-hydroxyacyl-CoA species through
CC addition of a water molecule to the double bond. Catalyzes the
CC hydration of medium- and short-chained fatty enoyl-CoA thioesters from
CC 4 carbons long (C4) up to C16 (By similarity). Has high substrate
CC specificity for crotonyl-CoA ((2E)-butenoyl-CoA) and moderate
CC specificity for acryloyl-CoA, 3-methylcrotonyl-CoA (3-methyl-(2E)-
CC butenoyl-CoA) and methacrylyl-CoA ((2E)-2-methylpropenoyl-CoA). Can
CC bind tiglyl-CoA (2-methylcrotonoyl-CoA), but hydrates only a small
CC amount of this substrate (By similarity). Plays a key role in the beta-
CC oxidation spiral of short- and medium-chain fatty acid oxidation. At a
CC lower rate than the hydratase reaction, catalyzes the isomerase
CC reaction of trans-3-enoyl-CoA species (such as (3E)-hexenoyl-CoA) to
CC trans-2-enoyl-CoA species (such as (2E)-hexenoyl-CoA), which are
CC subsequently hydrated to 3(S)-3-hydroxyacyl-CoA species (such as (3S)-
CC hydroxyhexanoyl-CoA) (By similarity). {ECO:0000250|UniProtKB:P14604,
CC ECO:0000250|UniProtKB:P30084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16107;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC EC=5.3.3.8; Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-hexenoyl-CoA = (2E)-hexenoyl-CoA; Xref=Rhea:RHEA:45736,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:84790;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45737;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26558, ChEBI:CHEBI:15377, ChEBI:CHEBI:57316,
CC ChEBI:CHEBI:57332; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26560;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxyisovaleryl-CoA = 3-methyl-(2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31079, ChEBI:CHEBI:15377, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:62555; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31081;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O;
CC Xref=Rhea:RHEA:26518, ChEBI:CHEBI:15377, ChEBI:CHEBI:57367,
CC ChEBI:CHEBI:58528; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:26520;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:45584, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:78611; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45586;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-2-methylpropenoyl-CoA + H2O = (S)-3-hydroxyisobutanoyl-
CC CoA; Xref=Rhea:RHEA:31175, ChEBI:CHEBI:15377, ChEBI:CHEBI:62500,
CC ChEBI:CHEBI:62611; Evidence={ECO:0000250|UniProtKB:P30084};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31176;
CC Evidence={ECO:0000250|UniProtKB:P30084};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxyhexanoyl-CoA = (2E)-hexenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:30547, ChEBI:CHEBI:15377, ChEBI:CHEBI:62075,
CC ChEBI:CHEBI:62077; Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30549;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxydecanoyl-CoA = (2E)-decenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:31191, ChEBI:CHEBI:15377, ChEBI:CHEBI:61406,
CC ChEBI:CHEBI:62616; Evidence={ECO:0000250|UniProtKB:P14604};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31193;
CC Evidence={ECO:0000250|UniProtKB:P14604};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P30084}.
CC -!- SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000250|UniProtKB:P14604}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P14604}.
CC -!- PTM: Acetylation of Lys-101 is observed in liver mitochondria from
CC fasted mice but not from fed mice. {ECO:0000269|PubMed:23576753}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK040391; BAC30583.1; -; mRNA.
DR EMBL; AK044954; BAC32157.1; -; mRNA.
DR EMBL; AK088018; BAC40099.1; -; mRNA.
DR EMBL; AK167404; BAE39493.1; -; mRNA.
DR EMBL; BC002178; AAH02178.1; -; mRNA.
DR EMBL; BC057971; AAH57971.1; -; mRNA.
DR EMBL; BC072658; AAH72658.1; -; mRNA.
DR CCDS; CCDS21964.1; -.
DR RefSeq; NP_444349.1; NM_053119.2.
DR AlphaFoldDB; Q8BH95; -.
DR SMR; Q8BH95; -.
DR BioGRID; 220286; 41.
DR IntAct; Q8BH95; 1.
DR MINT; Q8BH95; -.
DR STRING; 10090.ENSMUSP00000026538; -.
DR iPTMnet; Q8BH95; -.
DR PhosphoSitePlus; Q8BH95; -.
DR SwissPalm; Q8BH95; -.
DR REPRODUCTION-2DPAGE; Q8BH95; -.
DR CPTAC; non-CPTAC-3460; -.
DR EPD; Q8BH95; -.
DR jPOST; Q8BH95; -.
DR MaxQB; Q8BH95; -.
DR PaxDb; Q8BH95; -.
DR PeptideAtlas; Q8BH95; -.
DR PRIDE; Q8BH95; -.
DR ProteomicsDB; 277712; -.
DR Antibodypedia; 19426; 248 antibodies from 26 providers.
DR DNASU; 93747; -.
DR Ensembl; ENSMUST00000026538; ENSMUSP00000026538; ENSMUSG00000025465.
DR GeneID; 93747; -.
DR KEGG; mmu:93747; -.
DR UCSC; uc009kgx.1; mouse.
DR CTD; 1892; -.
DR MGI; MGI:2136460; Echs1.
DR VEuPathDB; HostDB:ENSMUSG00000025465; -.
DR eggNOG; KOG1680; Eukaryota.
DR GeneTree; ENSGT00940000157609; -.
DR InParanoid; Q8BH95; -.
DR OMA; IFKQTDA; -.
DR OrthoDB; 1221604at2759; -.
DR PhylomeDB; Q8BH95; -.
DR TreeFam; TF314497; -.
DR Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR Reactome; R-MMU-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR Reactome; R-MMU-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR Reactome; R-MMU-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR Reactome; R-MMU-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR Reactome; R-MMU-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 93747; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Echs1; mouse.
DR PRO; PR:Q8BH95; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BH95; protein.
DR Bgee; ENSMUSG00000025465; Expressed in brown adipose tissue and 268 other tissues.
DR Genevisible; Q8BH95; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043956; F:3-hydroxypropionyl-CoA dehydratase activity; IEA:RHEA.
DR GO; GO:0120092; F:crotonyl-CoA hydratase activity; IEA:RHEA.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:RHEA.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR Gene3D; 1.10.12.10; -; 1.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Fatty acid metabolism; Isomerase;
KW Lipid metabolism; Lyase; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..290
FT /note="Enoyl-CoA hydratase, mitochondrial"
FT /id="PRO_0000007412"
FT BINDING 98..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 101
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 101
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30084"
FT MOD_RES 115
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 115
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 204
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 217
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 217
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 71
FT /note="Q -> L (in Ref. 2; AAH02178)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="G -> R (in Ref. 2; AAH72658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31474 MW; 3E51E529CE756C68 CRC64;
MAALRALLPR ACSSLLSSVR CPELRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA
LCNGLIEELN QALETFEQDP AVGAIVLTGG DKAFAAGADI KEMQNRTFQD CYSSKFLSHW
DHITRVKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT
RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVEKLVE EAIQCAEKIA SNSKIVVAMA
KESVNAAFEM TLTEGNKLEK RLFYSTFATD DRREGMTAFV EKRKANFKDH
