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Database: UniProt
Entry: A0A1Q2YLY9_9ASCO
LinkDB: A0A1Q2YLY9_9ASCO
Original site: A0A1Q2YLY9_9ASCO 
ID   A0A1Q2YLY9_9ASCO        Unreviewed;       605 AA.
AC   A0A1Q2YLY9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PMKS-004031 {ECO:0000313|EMBL:GAV30517.1};
OS   Pichia membranifaciens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Pichia.
OX   NCBI_TaxID=4926 {ECO:0000313|EMBL:GAV30517.1, ECO:0000313|Proteomes:UP000186136};
RN   [1] {ECO:0000313|EMBL:GAV30517.1, ECO:0000313|Proteomes:UP000186136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KS47-1 {ECO:0000313|EMBL:GAV30517.1,
RC   ECO:0000313|Proteomes:UP000186136};
RA   Konishi M., Ishida M., Arakawa T., Kato Y., Horiuchi J.;
RT   "Whole genome shotgun sequence of Pichia membranifaciens KS47-1.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:GAV30517.1}.
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DR   EMBL; BDGI01000184; GAV30517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2YLY9; -.
DR   Proteomes; UP000186136; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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: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   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:UP000186136};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          38..141
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          245..372
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          449..528
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         516
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         518
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   605 AA;  68392 MW;  8CDF0E8B619C6765 CRC64;
     MMETAIKNEL VSNDMKSVTE QQAIKKLKAG FSNKPEITIS EYIFHRILQL GIKSVFGVPG
     DFNLKFLEHI YDVKELNWIG CCNELNAAYS ADAYGKTSGK MGVLLTTYGV GELSALNGVA
     GAYTEFAPLL HLVGTSALKL KRDPRTLNMH HLAGNRCTWK KSDHYVYEKV AENFSIDSAS
     IEDDPEEACE MVDRVILSVW RNSRPGYIFL PCDMAEMKVD VARLSIPIKL EYEFKRPADE
     VNAYVEKILD MMYKSKNMSI IADEFIRKFR MEDEMHAMLK KLDGKVNLYS TMFSKGLVDE
     EDPRFIGTYF GKYESPVAKI IESSDLVLHL GKFDNELNCG HFTFNLEQDK LIEFSPQYMQ
     IGKEFDDTVN MMEILPLLVE KLDGQKVSPA VKYERPKKSY ELAEPPREYP LTEVDLVKSL
     NKNIRSNDVL IVETCSFLFA VPDIKIRNAR VILQGYWASI GYALPATLGA SLALRDFNLP
     GRVITVEGDG SAQMSLQELS SMLRYNIDAT MLILNNSGYT IERVITGPYS SYNDINANWQ
     WGDMLKCFGD LKQEKSESFK VQNPAELDKT LGSENYANGK FKLLELILPM FDVPEKLTNA
     VSSAS
//
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