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
//