ID   ECHD1_RAT               Reviewed;         299 AA.
AC   Q6AYG5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 38-51, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (DEC-2006) to UniProtKB.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22016388; DOI=10.1074/jbc.m111.281527;
RA   Linster C.L., Noel G., Stroobant V., Vertommen D., Vincent M.F.,
RA   Bommer G.T., Veiga-da-Cunha M., Van Schaftingen E.;
RT   "Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite
RT   proofreading.";
RL   J. Biol. Chem. 286:42992-43003(2011).
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; BC079052; AAH79052.1; -; mRNA.
DR   RefSeq; NP_001007735.1; NM_001007734.1.
DR   RefSeq; XP_006227809.1; XM_006227747.3.
DR   RefSeq; XP_017444821.1; XM_017589332.1.
DR   AlphaFoldDB; Q6AYG5; -.
DR   SMR; Q6AYG5; -.
DR   STRING; 10116.ENSRNOP00000015440; -.
DR   iPTMnet; Q6AYG5; -.
DR   PhosphoSitePlus; Q6AYG5; -.
DR   jPOST; Q6AYG5; -.
DR   PaxDb; Q6AYG5; -.
DR   PRIDE; Q6AYG5; -.
DR   GeneID; 361465; -.
DR   KEGG; rno:361465; -.
DR   UCSC; RGD:1359654; rat.
DR   CTD; 55862; -.
DR   RGD; 1359654; Echdc1.
DR   VEuPathDB; HostDB:ENSRNOG00000011622; -.
DR   eggNOG; KOG1680; Eukaryota.
DR   HOGENOM; CLU_009834_7_6_1; -.
DR   InParanoid; Q6AYG5; -.
DR   OMA; HKQMGLV; -.
DR   OrthoDB; 1234730at2759; -.
DR   PhylomeDB; Q6AYG5; -.
DR   TreeFam; TF315986; -.
DR   PRO; PR:Q6AYG5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000011622; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q6AYG5; RN.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Lyase;
KW   Reference proteome.
FT   CHAIN           1..299
FT                   /note="Ethylmalonyl-CoA decarboxylase"
FT                   /id="PRO_0000273249"
FT   MOD_RES         209
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT   MOD_RES         209
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT   MOD_RES         293
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
SQ   SEQUENCE   299 AA;  32631 MW;  B74CCD89B663C42E CRC64;
     MAKSLLASSL SVRTKILQTG VSLYNTTHGF HEEEVKKILE QFPGGSIDLQ KKQNGIGILT
     LNNSNKMNAF SGAMMLQLLE RVIELENWTE GKGLIVHGAK NTFCSGSDLN AVKALSTPEN
     GVALSMFMQN TLTRFMRLPL ISVALVQGWA MGGGAELTTA CDFRLMTEES VIRFVHKEMG
     IVPSWGGASR LVEIIGSRQA LKVLSGTFKL DSKEALRIGL ADEVLQPSDE ATALEQAQEW
     LEQFVSGPAQ VIRGLKKSVC SGRELYLEEA LQNERDVLET LWGGPANLEA IAKKGKHTK