ID B5VFI6_YEAS6 Unreviewed; 446 AA.
AC B5VFI6;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=branched-chain-2-oxoacid decarboxylase {ECO:0000256|ARBA:ARBA00012227};
DE EC=4.1.1.72 {ECO:0000256|ARBA:ARBA00012227};
DE AltName: Full=Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase {ECO:0000256|ARBA:ARBA00029572};
GN ORFNames=AWRI1631_41580 {ECO:0000313|EMBL:EDZ73303.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ73303.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ73303.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ73303.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2;
CC Xref=Rhea:RHEA:21108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16182,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:35146; EC=4.1.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00001090};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Amino-acid degradation; Ehrlich pathway.
CC {ECO:0000256|ARBA:ARBA00005052}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:EDZ73303.1}.
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DR EMBL; ABSV01000358; EDZ73303.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VFI6; -.
DR UniPathway; UPA00866; -.
DR Proteomes; UP000008988; Unassembled WGS sequence.
DR GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0000955; P:amino acid catabolic process via Ehrlich pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02005; TPP_PDC_IPDC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 37..161
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 243..351
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 446 AA; 50404 MW; 81EDD5EE8114A4CB CRC64;
MGMPVNQVNL PIESARLNTP LDLQLHKNDP DVEKEVISRI LSFIYKSQNP AIIVDACTSR
QNLIEETKEL CNRLKFPVFV TPMGKGTVNE TDPQFGGVFT GSISAPEVRE VVDFADFIIV
IGCMLSEFST STFHFQYKTK NCALLYSTSV KLKNATYPDL SIKLLLQKLL ANLDESKLSY
QPSEQPSMMV PRPYPAGNVL LRQEWVWNEI SHWFQPGDII ITETGASAFG VNQTRFPVNT
LGISQALWGS VGYTMGACLG AEFAVQEINK DKFPATKHRV ILFMGDGAFQ LTVQELSTIV
KWGLTPYIFV MNNQGYSVDR FLHHRSDASY YDIQPWNYLG LLRVFGCTNY ETKKIITVGE
FRSMISDPNF ATNDKIRMIE IMLPPRDVPQ ALLDRWVVEK EQSKQVQEEN ENSSAVDTPT
PEFQPLLKKI KLDTDLISPP YYQGPS
//
