ID   ECHD1_XENLA             Reviewed;         299 AA.
AC   Q5HZQ8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-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. 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}.
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DR   EMBL; BC088922; AAH88922.1; -; mRNA.
DR   RefSeq; NP_001088953.1; NM_001095484.1.
DR   AlphaFoldDB; Q5HZQ8; -.
DR   SMR; Q5HZQ8; -.
DR   GeneID; 496330; -.
DR   KEGG; xla:496330; -.
DR   CTD; 496330; -.
DR   Xenbase; XB-GENE-958561; echdc1.L.
DR   OMA; HKQMGLV; -.
DR   OrthoDB; 1234730at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 496330; Expressed in egg cell and 19 other tissues.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..299
FT                   /note="Ethylmalonyl-CoA decarboxylase"
FT                   /id="PRO_0000416273"
SQ   SEQUENCE   299 AA;  32656 MW;  189E9519536368FA CRC64;
     MGIFVWRSSL SMTNIRWLHH RCLSLYNSSH GFNEAKIKKK LAQFTGGSVD LSKSDDGIAE
     ICINNPTRMN AFTGTMMIEL EERISDLENW QDGKGLIVYG AENTFCSGSD LNAVKAISNP
     QEGMMMCMLM QNTLTRLQRL PLVSVALIQG KALGGGAELC TACDFRLMTE GSEIRFVHKQ
     MGLVPGWGGA ARLIHIVGSR HALKLLSGAP RVQPENALEL GLADNILTGT EAGVLSEAKN
     WIMPYIKGPS DVTRAVKKVI ISGREQNLED ALRTEKEIFG TVWGGLANLQ ALAKGTKHK