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Database: UniProt
Entry: A0A420YIR5_9PEZI
LinkDB: A0A420YIR5_9PEZI
Original site: A0A420YIR5_9PEZI 
ID   A0A420YIR5_9PEZI        Unreviewed;       569 AA.
AC   A0A420YIR5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=DL546_005490 {ECO:0000313|EMBL:RKU47764.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU47764.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU47764.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU47764.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) 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|PIRSR:PIRSR036565-2};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|ARBA:ARBA00001920};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:RKU47764.1}.
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DR   EMBL; QVQW01000007; RKU47764.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420YIR5; -.
DR   STRING; 177199.A0A420YIR5; -.
DR   Proteomes; UP000275385; 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; 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:SF6; PYRUVATE DECARBOXYLASE C186.09-RELATED; 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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275385};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          8..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          206..302
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          413..536
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         443
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         470
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   569 AA;  61747 MW;  C9B315B8C250FB38 CRC64;
     MTSTPEYTIG DYLADRLAQI GCRHHFVVPG DYNLILLDKL QSNPALKEIG CANELNCSMA
     AEGYARANGV SACVVTFSVG AISAFNGTGS AYSENLPLIL ISGSPNTNDA GQFHMLHHTL
     ATNDFSYQIE MAKKITCCAV AVGRPEEAPR LIDRAIRAAL LSRKPCYIEI PTNLAGAHCV
     RPGPISAVID PVHSDNATLI AAADCASDYL RGKQKPVILV GPKLGRAPGA KKELIRFAEA
     LGCAVAVQPA AKGMFPEDHP QFVGIFWGTI STLAADAIIA WADAIICVGT IFTDYSTVGW
     TAMPSIPLMV AEMDHVSFPG AHFSRVRLSE FLNHLAQEVT ANDATMVEYG RLRPDPIMVH
     TAAPEDALTR KEITRQVQEL LCERTTLFVE TGDSWFNGIS LRLPPGADFE IEMQWGHIGW
     SIPAAFGYAI GHRDRRVIVM VGDGSFQVTA QEVSQMVRYK LPITILLINN RGYTIEVEIH
     DGSYNRIKNW DYAKLVEAFN AEDGKAAGYK ANTAGELASA IERAGKNTEG PTLIECTIDQ
     DDCTRELITW GHYVAKANAR PPVQPGGLF
//
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