ID W2YNB2_PHYPR Unreviewed; 344 AA.
AC W2YNB2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ORFNames=F442_15833 {ECO:0000313|EMBL:ETP36133.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP36133.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP36133.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP36133.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP36133.1}.
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DR EMBL; ANIY01003337; ETP36133.1; -; Genomic_DNA.
DR EMBL; ANIY01003337; ETP36134.1; -; Genomic_DNA.
DR AlphaFoldDB; W2YNB2; -.
DR EnsemblProtists; ETP36133; ETP36133; F442_15833.
DR EnsemblProtists; ETP36134; ETP36134; F442_15833.
DR Proteomes; UP000018948; Unassembled WGS sequence.
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:UP000018948}.
SQ SEQUENCE 344 AA; 37007 MW; 31D165EBCC3D18EB CRC64;
MLHGVGFGYA VSKSRLALSR LKASPQQARG MFSFINDSEQ DGKSLVALSR EALRGLGKRD
DHVTLHLPFL PSPAGSKNTL PVQSTRLPLG FETLQKTAVL EIDNPSARNA LSGNMMAQLA
DIVTLLEDPK VHDKLNVVVL RGTGGWFCAG ANLRVARDEL NSREAGAAMG ALMVDTLTRF
RRLPLVSIAA IEGGAFGGGA ELATACDFRI IEGNAVIQFV QSRMGVIPGW GGGARLYKIV
GRQNALRLLC TAERISPDRA LQLKLVDEIF FATDEESSNT GITSFVEAFD AIVPAVSHGA
KRVINNADDV SLDDVLKYEH DVFKTLWGGP ANLEALEKAL SKKK
//
