ID   ECHD1_PONAB             Reviewed;         301 AA.
AC   Q5R4W0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR861131; CAH93206.1; -; mRNA.
DR   EMBL; CR925967; CAI29618.1; -; mRNA.
DR   RefSeq; NP_001126886.1; NM_001133414.1.
DR   RefSeq; XP_009240496.1; XM_009242221.1.
DR   AlphaFoldDB; Q5R4W0; -.
DR   SMR; Q5R4W0; -.
DR   STRING; 9601.ENSPPYP00000024266; -.
DR   Ensembl; ENSPPYT00000019781; ENSPPYP00000019030; ENSPPYG00000016995.
DR   GeneID; 100173900; -.
DR   KEGG; pon:100173900; -.
DR   CTD; 55862; -.
DR   eggNOG; KOG1680; Eukaryota.
DR   GeneTree; ENSGT00880000138038; -.
DR   InParanoid; Q5R4W0; -.
DR   OrthoDB; 1234730at2759; -.
DR   Proteomes; UP000001595; Chromosome 6.
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   Acetylation; Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Ethylmalonyl-CoA decarboxylase"
FT                   /id="PRO_0000273248"
FT   MOD_RES         211
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT   MOD_RES         211
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT   MOD_RES         295
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
SQ   SEQUENCE   301 AA;  32985 MW;  EC74C79DA2FB6FD8 CRC64;
     MAKSLLKTSS LSGRTKLLHQ TGLSLYSTSH GFYEEEVKKT LQQFPGGSID LQKEDNGIGI
     LTLNNPSKMN AFSGVMMLQL LEKVIELENW TEGKGLIVRG AKNTFSSGSD LNAVKSLGTP
     EDGMAVCMFM QNTLTRFMRL PLISVALVQG WALGGGAEFT TACDFRLMTP ESKIRFVHKE
     MGIIPSWGGT TRLVEIIGSR QALKVLSGAL KLDSKNALNI GMVEEVLQSS DETKSLEEAQ
     EWLKQFIQGP PEVIRALKKS VCSGRELYLE EALQNERDLL GTVWGGPANL EAIAKKGKFN
     K