ECHD1_CHICK
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 03-AUG-2022, entry version 45.
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. Also has methylmalonyl-CoA decarboxylase
CC activity at lower level. {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 -!- 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 STRING; 9031.ENSGALP00000023891; -.
DR PaxDb; F1NB38; -.
DR VEuPathDB; HostDB:geneid_769021; -.
DR eggNOG; KOG1680; Eukaryota.
DR InParanoid; F1NB38; -.
DR OrthoDB; 1234730at2759; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 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
