ID ECHD1_BOVIN Reviewed; 306 AA. AC Q2HJD5; F1MDK4; Q58DU9; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 24-JAN-2024, entry version 85. DE RecName: Full=Ethylmalonyl-CoA decarboxylase; DE EC=4.1.1.94 {ECO:0000250|UniProtKB:Q9D9V3}; DE AltName: Full=Enoyl-CoA hydratase domain-containing protein 1; DE AltName: Full=Methylmalonyl-CoA decarboxylase; DE Short=MMCD; GN Name=ECHDC1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D., RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G., RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Ascending colon; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Decarboxylates ethylmalonyl-CoA, a potentially toxic CC metabolite, to form butyryl-CoA, suggesting it might be involved in CC metabolite proofreading. Acts preferentially on (S)-ethylmalonyl-CoA CC but has also some activity on the (R)-isomer. Also has methylmalonyl- CC CoA decarboxylase activity at lower level. CC {ECO:0000250|UniProtKB:Q9D9V3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2S)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2; CC Xref=Rhea:RHEA:32131, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57371, ChEBI:CHEBI:60909; EC=4.1.1.94; CC Evidence={ECO:0000250|UniProtKB:Q9D9V3}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32132; CC Evidence={ECO:0000250|UniProtKB:Q9D9V3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-methylmalonyl-CoA + H(+) = CO2 + propanoyl-CoA; CC Xref=Rhea:RHEA:61340, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57392; EC=4.1.1.94; CC Evidence={ECO:0000250|UniProtKB:Q9D9V3}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61341; CC Evidence={ECO:0000250|UniProtKB:Q9D9V3}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2; CC Xref=Rhea:RHEA:59540, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57371, ChEBI:CHEBI:85316; EC=4.1.1.94; CC Evidence={ECO:0000250|UniProtKB:Q9D9V3}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59541; CC Evidence={ECO:0000250|UniProtKB:Q9D9V3}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q9D9V3}. 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; BT021498; AAX46345.1; -; mRNA. DR EMBL; DAAA02025518; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC105549; AAI05550.1; -; mRNA. DR RefSeq; NP_001030492.1; NM_001035415.1. DR AlphaFoldDB; Q2HJD5; -. DR SMR; Q2HJD5; -. DR STRING; 9913.ENSBTAP00000056819; -. DR PaxDb; 9913-ENSBTAP00000005072; -. DR PeptideAtlas; Q2HJD5; -. DR Ensembl; ENSBTAT00000084959.1; ENSBTAP00000056819.1; ENSBTAG00000003887.4. DR GeneID; 536284; -. DR KEGG; bta:536284; -. DR CTD; 55862; -. DR VEuPathDB; HostDB:ENSBTAG00000003887; -. DR VGNC; VGNC:28306; ECHDC1. DR eggNOG; KOG1680; Eukaryota. DR GeneTree; ENSGT00880000138038; -. DR InParanoid; Q2HJD5; -. DR OMA; AQRTKHK; -. DR OrthoDB; 50856at2759; -. DR Proteomes; UP000009136; Chromosome 9. DR Bgee; ENSBTAG00000003887; Expressed in zone of skin and 106 other cell types or tissues. DR ExpressionAtlas; Q2HJD5; baseline and differential. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB. DR GO; GO:0004492; F:methyl/ethyl malonyl-CoA decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central. DR CDD; cd06558; crotonase-like; 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 PANTHER; PTHR11941; ENOYL-COA HYDRATASE-RELATED; 1. DR PANTHER; PTHR11941:SF27; ETHYLMALONYL-COA DECARBOXYLASE; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Lyase; Reference proteome. FT CHAIN 1..306 FT /note="Ethylmalonyl-CoA decarboxylase" FT /id="PRO_0000273245" FT MOD_RES 216 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9D9V3" FT MOD_RES 216 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9D9V3" FT CONFLICT 176 FT /note="E -> Q (in Ref. 1; AAX46345)" FT /evidence="ECO:0000305" SQ SEQUENCE 306 AA; 33542 MW; 380866BE4ED86C88 CRC64; MELKQEMASL LKTSPNAVKK RLLHQIGLSL YNTSHGFHEE EVKKKLEQFP GGSIDLQKEN SGIGILTLNN PSKMNAFSGV MMLQLLEKVI ELENWTEGKG LIIRGAKNTF SSGSDLNAVK ALGTPEDGMA VCMFMQNTLT RFMRLPLISV ALVQGRALGG GAEVTTACDF RLMTTESEIR FVHKEMGIIP SWGGATRLVE IIGGRQALKV LSGALKLDSE KALNIGMVDD ILPSSDETEC LKEAQEWLQQ FIKGPPEVIR ALKKSVSSCK ELCLEEALQR ERDILGTVWG GPANLEAVAR KGKFNK //