ID   ECHD1_XENTR             Reviewed;         299 AA.
AC   Q28C91; F6UNG1; Q0VFD0; Q5M791;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
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; ORFNames=TGas092k23.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Gastrula, and Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) 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}.
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DR   EMBL; CR942395; CAJ83594.1; -; mRNA.
DR   EMBL; AAMC01103784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC088780; AAH88780.1; -; mRNA.
DR   EMBL; BC118874; AAI18875.1; -; mRNA.
DR   EMBL; BC170562; AAI70562.1; -; mRNA.
DR   EMBL; BC170919; AAI70919.1; -; mRNA.
DR   RefSeq; NP_001037862.1; NM_001044397.1.
DR   AlphaFoldDB; Q28C91; -.
DR   SMR; Q28C91; -.
DR   STRING; 8364.ENSXETP00000010823; -.
DR   PaxDb; 8364-ENSXETP00000061979; -.
DR   GeneID; 496886; -.
DR   KEGG; xtr:496886; -.
DR   AGR; Xenbase:XB-GENE-958554; -.
DR   CTD; 55862; -.
DR   Xenbase; XB-GENE-958554; echdc1.
DR   eggNOG; KOG1680; Eukaryota.
DR   HOGENOM; CLU_009834_7_6_1; -.
DR   InParanoid; Q28C91; -.
DR   OrthoDB; 50856at2759; -.
DR   TreeFam; TF315986; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   ExpressionAtlas; Q28C91; baseline.
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   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   Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..299
FT                   /note="Ethylmalonyl-CoA decarboxylase"
FT                   /id="PRO_0000416274"
SQ   SEQUENCE   299 AA;  32907 MW;  A0452C4A22C4DDF0 CRC64;
     MGIFVCRNSL RMLNVRWLYH RCLSLYNSNH GFNEAKIKEK LAQFTGGSVD LSKMDNGIAE
     ICINNPSRMN AFTGTMMIEL EERISDLENW KNGKGLIVYG AENTFCSGSD LNAVKAISNP
     QEGMMMCMLM QNTLTRLQRL PLISVALIQG KALGGGAELC TACDFRLMTE GSEIRFVHKQ
     MGLVPGWGGA ARLIHLIGSR HALKLLSGAL RVHPENALEL GLADNILLGT EDGFLSEAEN
     WIMPYIKGPS DVSRAVKKVI ISGREQKLED ALRTEKEIFG TVWGGLANLQ ALAKGTKHK
//