ID A0A0A8X333_9BACI Unreviewed; 256 AA.
AC A0A0A8X333;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMD00020551_1835 {ECO:0000313|EMBL:GAM13689.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM13689.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM13689.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM13689.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-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:GAM13689.1}.
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DR EMBL; BASE01000040; GAM13689.1; -; Genomic_DNA.
DR RefSeq; WP_041965519.1; NZ_BASE01000040.1.
DR AlphaFoldDB; A0A0A8X333; -.
DR STRING; 1321606.SAMD00020551_1835; -.
DR OrthoDB; 9775794at2; -.
DR Proteomes; UP000031014; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004492; F:methyl/ethyl malonyl-CoA decarboxylase activity; IEA:RHEA.
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 Lyase {ECO:0000313|EMBL:GAM13689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031014}.
SQ SEQUENCE 256 AA; 28264 MW; 004D38D84606E60A CRC64;
MDPYIISKEK NGVLLFTINR PDRRNAINYE VMSGLEKAID MAAGNDIKVF AITGAGDQAF
CSGGDLSAFH SLKTETQAYG MLSRMAGILY KLLVLPKPTI AILNGSAVGG GCEIASACDF
RIGREGMKAG FVQGNLAITT GWGGGSILLE KLPQNIAMKM LLDAKIHTAE ELRDFGFIHQ
IYKDDPIDAC LSFMSGSLDK ETTVLEAYKT MLNKKWKLLS MRERMEEEAA RCAVLWEDDA
HHKKVDEFMN KKNKNN
//
