ID A0A135T6W3_9PEZI Unreviewed; 638 AA.
AC A0A135T6W3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN ORFNames=CSAL01_01799 {ECO:0000313|EMBL:KXH43883.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH43883.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH43883.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH43883.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001041};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KXH43883.1}.
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DR EMBL; JFFI01002087; KXH43883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135T6W3; -.
DR STRING; 1209931.A0A135T6W3; -.
DR OrthoDB; 1328249at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KXH43883.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 618..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 66971 MW; 5622FC28FE73D49D CRC64;
MAFQVRQPKN RELLGGDLLA QSLAHLGATT AFGIHGGHLD SFLIAAVEAD IKLIDVRHET
VAVQAAEGWA KVKGNDAPGV CFITANSGFC NGLPGLSTAF ADRSPVFCIT SSPPLRDAET
NTLQGFHDQV VLAKAVTKFA HRVTNGSEIP RIVSLAWRAT TAGAPGPVLV DFPIDVLFTP
VEIDSVAWGS ITAPPVSLPA PDAGAVEKAM RLWGEAKRPV ILVSTGAARA ADEVVKLAEA
TNTPIFHSPK FSTSIKRSDP LFGGVATRLP FLRAQGPAPD FVLLLGARTG FLIGGRSGAI
VPNENEAKVV QVDLDGSEIG RSRKIDVGIV SDVGLAAQAL AAAASKSSVK ANSDWVDKAM
ALKKPSVHSA GNEDDPVIIE ENDRIHPYHG VKAFFQALPE DSILCMDGGE CGGWALQSLN
EARAGLSMVT TGYLGFLGNG FGYSLGAAVA APDKLVVNLH GDGSAGFHIG ELDTYAKFSL
NILTVVVNNS VWGMSQAGQN MIYGEKTLQR PCVAMNPKVK YEVVAQGFGC DGAVVDVVKE
NGASNGPKTL ESVKVAVRTL TSAKQPSLLN LKVSDVPYQN TTKAMVGGSS DPNIIVVPYY
DNLPRPYYKK SEQGAAASAN ATSAPKEESF VEGHGTIQ
//