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ECHD1_BOVIN
ID   ECHD1_BOVIN             Reviewed;         306 AA.
AC   Q2HJD5; F1MDK4; Q58DU9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-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; BT021498; AAX46345.1; -; mRNA.
DR   EMBL; DAAA02025518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC105549; AAI05550.1; -; mRNA.
DR   RefSeq; NP_001030492.1; NM_001035415.1.
DR   AlphaFoldDB; Q2HJD5; -.
DR   SMR; Q2HJD5; -.
DR   STRING; 9913.ENSBTAP00000005072; -.
DR   PaxDb; Q2HJD5; -.
DR   PeptideAtlas; Q2HJD5; -.
DR   PRIDE; Q2HJD5; -.
DR   Ensembl; ENSBTAT00000084959; ENSBTAP00000056819; ENSBTAG00000003887.
DR   GeneID; 536284; -.
DR   KEGG; bta:536284; -.
DR   CTD; 55862; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003887; -.
DR   VGNC; VGNC:28306; ECHDC1.
DR   eggNOG; KOG1680; Eukaryota.
DR   GeneTree; ENSGT00880000138038; -.
DR   InParanoid; Q2HJD5; -.
DR   OMA; HKQMGLV; -.
DR   OrthoDB; 1234730at2759; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000003887; Expressed in zone of skin and 106 other tissues.
DR   ExpressionAtlas; Q2HJD5; baseline and differential.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..306
FT                   /note="Ethylmalonyl-CoA decarboxylase"
FT                   /id="PRO_0000273245"
FT   MOD_RES         216
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT   MOD_RES         216
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D9V3"
FT   CONFLICT        176
FT                   /note="E -> Q (in Ref. 1; AAX46345)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  33542 MW;  380866BE4ED86C88 CRC64;
     MELKQEMASL LKTSPNAVKK RLLHQIGLSL YNTSHGFHEE EVKKKLEQFP GGSIDLQKEN
     SGIGILTLNN PSKMNAFSGV MMLQLLEKVI ELENWTEGKG LIIRGAKNTF SSGSDLNAVK
     ALGTPEDGMA VCMFMQNTLT RFMRLPLISV ALVQGRALGG GAEVTTACDF RLMTTESEIR
     FVHKEMGIIP SWGGATRLVE IIGGRQALKV LSGALKLDSE KALNIGMVDD ILPSSDETEC
     LKEAQEWLQQ FIKGPPEVIR ALKKSVSSCK ELCLEEALQR ERDILGTVWG GPANLEAVAR
     KGKFNK
 
 
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