ECHD1_DANRE
ID ECHD1_DANRE Reviewed; 302 AA.
AC F1R6N4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 53.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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; AL929535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1R6N4; -.
DR SMR; F1R6N4; -.
DR STRING; 7955.ENSDARP00000060189; -.
DR PaxDb; F1R6N4; -.
DR ZFIN; ZDB-GENE-050522-370; echdc1.
DR eggNOG; KOG1680; Eukaryota.
DR InParanoid; F1R6N4; -.
DR PRO; PR:F1R6N4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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 3: Inferred from homology;
KW Cytoplasm; Lyase; Reference proteome.
FT CHAIN 1..302
FT /note="Ethylmalonyl-CoA decarboxylase"
FT /id="PRO_0000416272"
SQ SEQUENCE 302 AA; 32326 MW; 5E07A68444979529 CRC64;
MSMWGAVRCR LIQTRSAVRK ILQQNRAFCS GSSVGIREKL LAFPGGSVEL QKLQESGIAV
LTVSNPPARM NAFSGCMMLE LEQRVNELEI WTEGKAVIVQ GAAGNFCSGS DLNAVRAIAN
PHDGMKMCEF MQNTLARLLR LPLISVALVE GRALGGGAEL TTACDFRLMT SDAVIQFVHK
HMGLVPGWGG AARLVGIIGS RNALKLLSGA RKVDPDYGKQ MGLVDEVLQC SSGEGKALAH
AEHWIAPFIK GPAPVIQAIK KVVVSGRELS LDEALKCERS VFGTVWGGPA NLEALASKPK
HK
