ID ECHD1_CHICK Reviewed; 298 AA. AC F1NB38; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 2. DT 02-SEP-2026, entry version 56. 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 Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl; RX PubMed=15592404; DOI=10.1038/nature03154; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V., RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., RA Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide unique RT perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). 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 also has 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(+) = propanoyl-CoA + CO2; 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; AADN02001706; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001707; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001708; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001709; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001710; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001711; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001713; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001714; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001715; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001718; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001720; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AADN02001721; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F1NB38; -. DR SMR; F1NB38; -. DR FunCoup; F1NB38; 1504. DR STRING; 9031.ENSGALP00000070409; -. DR PaxDb; 9031-ENSGALP00000070409; -. DR VEuPathDB; HostDB:geneid_769021; -. DR eggNOG; KOG1680; Eukaryota. DR InParanoid; F1NB38; -. DR OrthoDB; 448450at2759; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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; ISS:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central. DR CDD; cd06558; crotonase-like; 1. DR FunFam; 3.90.226.10:FF:000040; Ethylmalonyl-CoA decarboxylase 1; 1. DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 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 3: Inferred from homology; KW Cytoplasm; Lyase; Reference proteome. FT CHAIN 1..298 FT /note="Ethylmalonyl-CoA decarboxylase" FT /id="PRO_0000416271" SQ SEQUENCE 298 AA; 32517 MW; 420ED5340D62D0A6 CRC64; MAVFLWRNLF QTTKARMLQQ RRASLYNGAH DYDEELIKKK LQQFAGGSIN LSKEHSGIGI LTLNNSRLMN AFTGTMMLEL QERVTELENW KDGKGLIICG AGNTFCSGSD LNAVKAISNS QDGMNMCMFM QNTLTRLMRL PLISIALIQG KALGGGAELT TACDFRLMTP GSEIRFVHKH MGLVPGWGGA ARLVRIIGSR AALQLLSRAH GVDPERALHL GLSEGTLSSS DETGSLEEAR AWLSQYTEGP ASVIQAVKKV VTAGRELPLE AALRTEKDVF GTVWGGPANL EALTRRQK //