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Database: UniProt
Entry: A0A0D2CSE6_9EURO
LinkDB: A0A0D2CSE6_9EURO
Original site: A0A0D2CSE6_9EURO 
ID   A0A0D2CSE6_9EURO        Unreviewed;       620 AA.
AC   A0A0D2CSE6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=PV07_00897 {ECO:0000313|EMBL:KIW34098.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW34098.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW34098.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW34098.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) 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=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}.
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DR   EMBL; KN847040; KIW34098.1; -; Genomic_DNA.
DR   RefSeq; XP_016254314.1; XM_016387386.1.
DR   AlphaFoldDB; A0A0D2CSE6; -.
DR   STRING; 569365.A0A0D2CSE6; -.
DR   GeneID; 27340091; -.
DR   VEuPathDB; FungiDB:PV07_00897; -.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   OrthoDB; 2067532at2759; -.
DR   Proteomes; UP000054466; 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:SF11; PYRUVATE 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   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:UP000054466};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..114
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          206..314
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          422..544
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          182..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         478
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         505
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         507
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   620 AA;  67966 MW;  DEF057E564C7359F CRC64;
     MVSLGGRTTV AKYLFTRLRQ QGVHAIHGVP GDFTLKALDY LPQAGVKWVG TCNELSAGYA
     ADGYARVRGL GALLTTYGVG ELSAINAVAG SFSEHVPVVS IVGTPQRRLQ DERKNVHHTL
     GDGRPRVFAE IARHVTVAQA NLVDEASAAE EIDRTIEAAL RESRPAYIEL PADMVAKEVD
     SARLEEPLPS QTSTGGDDED REMRLVDDLM KRIYAAKQPL LLVDSGGGVR QLRSEINDFV
     SASGIPTLCM PSGNGMVDHS LPNYYGVHSG PVGQIDTMPY VQGADLVIAF GPMFSDTQTL
     SWKVVPEPAK TITLAKNSIH DPTSPKSGGT KTDRIELRRF LTRLTQQIDR SKTASPDVAC
     LGDFRTVQPP AFAQASVDLD APIDQTSFYL RLSAYLRPYD VVVLGNATPI LGGRDLVLPT
     GAQMIASGQW FSIGHMLPLT MGASLARRHQ HQHQRRRRPH ETEANSGGGG RTILLDGDGG
     FQVTAQELGT MIRYKIPATI FLVNNAGYAY ERQIHGMHED YNDLAPWRYQ DLARTFGASE
     AQLSATAPRR ASEETVDDGD DDYYPVRNYE VATWRHLEQL LANEQFCRGR GLHFVDVRLG
     KFDVPEKFKV VFQRAGESLG
//
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