ID G3NRW9_GASAC Unreviewed; 310 AA.
AC G3NRW9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Ethylmalonyl-CoA decarboxylase {ECO:0000256|ARBA:ARBA00039903};
DE EC=4.1.1.94 {ECO:0000256|ARBA:ARBA00038883};
DE AltName: Full=Enoyl-CoA hydratase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042182};
DE AltName: Full=Methylmalonyl-CoA decarboxylase {ECO:0000256|ARBA:ARBA00042052};
GN Name=ECHDC1 {ECO:0000313|Ensembl:ENSGACP00000008086.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000008086.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000008086.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000008086.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-ethylmalonyl-CoA + H(+) = butanoyl-CoA + CO2;
CC Xref=Rhea:RHEA:59540, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:85316; EC=4.1.1.94;
CC Evidence={ECO:0000256|ARBA:ARBA00036541};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59541;
CC Evidence={ECO:0000256|ARBA:ARBA00036541};
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:0000256|ARBA:ARBA00036343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32132;
CC Evidence={ECO:0000256|ARBA:ARBA00036343};
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:0000256|ARBA:ARBA00036425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61341;
CC Evidence={ECO:0000256|ARBA:ARBA00036425};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254, ECO:0000256|RuleBase:RU003707}.
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DR AlphaFoldDB; G3NRW9; -.
DR STRING; 69293.ENSGACP00000008086; -.
DR Ensembl; ENSGACT00000008105.1; ENSGACP00000008086.1; ENSGACG00000006095.1.
DR eggNOG; KOG1680; Eukaryota.
DR GeneTree; ENSGT00880000138038; -.
DR InParanoid; G3NRW9; -.
DR OMA; AQRTKHK; -.
DR TreeFam; TF315986; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000006095; Expressed in muscle tissue and 11 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd06558; crotonase-like; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR PANTHER; PTHR11941; ENOYL-COA HYDRATASE-RELATED; 1.
DR PANTHER; PTHR11941:SF27; ETHYLMALONYL-COA DECARBOXYLASE; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
SQ SEQUENCE 310 AA; 32807 MW; F4FDCCD0E6764EB7 CRC64;
MALCALRRRL LRSSCAAWSR LLQRPSSGCV YSSVHGFHQD EITEKLQAFP GGSVDLLQQE
SGIAVLTINY PSRMNAFSGS MMVELEERVS QLESWTDGKG VIVRGADGTF CSGSDLTAVR
AISNPQDGMK MCMFMQNALT RLLRLPLISV ALVEGRALGG GAELTTACDF RLMASGSVIQ
FVHKHMGLVP GWGGAARLTR IVGSRNALKL LGGALKVDPE LGLQIGLADG VVEAPQAAEG
GAGVVLQQAE NWLSHYAGGA APVIRAVKKV VLSGGELPLS EALRTEKDVF GTVWGGPANL
QALASKSKHR
//