ID M4WIW8_YEASX Unreviewed; 635 AA.
AC M4WIW8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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};
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932 {ECO:0000313|EMBL:AGI16847.1};
RN [1] {ECO:0000313|EMBL:AGI16847.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EC1118 {ECO:0000313|EMBL:AGI16847.1};
RA Liu X., Lin J., Guo L., Wen Y., Xu X., Chen B.;
RT "Cloning of ARO8, ARO10 and ADH3 genes from Saccharomyces cerevisiae
RT strains.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
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, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KC422720; AGI16847.1; -; Genomic_DNA.
DR AlphaFoldDB; M4WIW8; -.
DR VEuPathDB; FungiDB:YDR380W; -.
DR UniPathway; UPA00866; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047214; TPP_PDC_IPDC.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF3; TRANSAMINATED AMINO ACID DECARBOXYLASE; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
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, ECO:0000256|PIRSR:PIRSR036565-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:AGI16847.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 462..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 244..373
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 444..571
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 49
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between two
FT neighboring subunits"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT BINDING 145
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between two
FT neighboring subunits"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT BINDING 196
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
FT BINDING 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 541
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 545
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_label="1"
FT /ligand_note="substrate; ligand shared between two
FT neighboring subunits"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-1"
SQ SEQUENCE 635 AA; 71418 MW; C16EA13B001949A3 CRC64;
MAPVTIEKFV NQEERHLVSN RSATIPFGEY IFKRLLSIDT KSVFGVPGDF NLSLLEYLYS
PSVESAGLRW VGTCNELNAA YAADGYSRYS NKIGCLITTY GVGELSALNG IAGSFAENVK
VLHIVGVAKS IDSRSSNFSD RNLHHLVPQL HDSNFKGPNH KVYHDMVKDR VACSVAYLED
IETACDQVDN VIRDIYKYSK PGYIFVPADF ADMSVTCDNL VNVPRISQQD CIVYPSENQL
SDIINKITSW IYSSKTPAIL GDVLTDRYGV SNFLNKLICK TGIWNFSTVM GKSVIDESNP
TYMGQYNGKE GLKQVYEHFE LCDLVLHFGV DINEINNGHY TFTYKPNAKI IQFHPNYIRL
VDTRQGNEQM FKGINFAPIL KELYKRIDVS KLSFQYDSNV TQYTNETMRL EDPTNGQSSI
ITQVHLQKTM PKFLNPGDVV VCETGSFQFS VRDFAFPSQL KYISQGFFLS IGMALPAALG
VGIAMQDHSN AHINGGNVKE DYKPRLILFE GDGAAQMTIQ ELSTILKCNI PLEVIIWNNN
GYTIERAIMG PTRSYNDVMS WKWTKLFEAF GDFDGKYTNS TLIQCPSKLA LKLEELKNSN
KRSGIELLEV KLGELDFPEQ LKCMVEAAAL KRNKK
//
