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Database: UniProt
Entry: A0A135T6W3_9PEZI
LinkDB: A0A135T6W3_9PEZI
Original site: A0A135T6W3_9PEZI 
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
//
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