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Database: UniProt
Entry: A0A0F4YPV3_TALEM
LinkDB: A0A0F4YPV3_TALEM
Original site: A0A0F4YPV3_TALEM 
ID   A0A0F4YPV3_TALEM        Unreviewed;       546 AA.
AC   A0A0F4YPV3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
GN   ORFNames=T310_5700 {ECO:0000313|EMBL:KKA20279.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20279.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA20279.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20279.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) 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:KKA20279.1}.
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DR   EMBL; LASV01000275; KKA20279.1; -; Genomic_DNA.
DR   RefSeq; XP_013326891.1; XM_013471437.1.
DR   AlphaFoldDB; A0A0F4YPV3; -.
DR   STRING; 1408163.A0A0F4YPV3; -.
DR   GeneID; 25318040; -.
DR   OrthoDB; 1000728at2759; -.
DR   Proteomes; UP000053958; 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:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-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; 2.
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, ECO:0000313|EMBL:KKA20279.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:KKA20279.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          38..91
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          185..319
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          383..502
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   BINDING         425
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ   SEQUENCE   546 AA;  60613 MW;  300995E6F7B6F9F0 CRC64;
     MASFDIVTRE LKQPIDVAEY LYRRLYEVGI RSVHGVPGYA ADGYARVNGI SALVTTFGVG
     ELSALNAIAG AYSEYVPIVH IVGQPSTIAQ RDGRLLHHTL GNGDFNVFVE MSAGISCAVA
     RLDDLHDTAT LIDNAIRECW IRSRPVYIAL PMDIVQKKVE GERLKTPIDL TRPPNDPEKE
     EYVVDVILKY LHEAKNPIIL VDACAIRHHV LDEVNDLIEA SGLPTFVAPM GKGAVDETHR
     NFGGVYAGDG SNQGVREVVE SSDLILSIGA IKSDFNTAGF TYRIGQLHTI DFHSTYVRVR
     YSEYPDINMK GVLRKVIQRM RKLNTRPIPK ITNAIPPAEQ TSTDSTITHA WLWPTVGQWL
     RENDIVITET GTANFGIWET RFPKGVTALS QVLWGSIGYS VGACQGAALA AKERNNRRTI
     LFVGDGSFQF TVQEMSTILR KGLKPIVFVI CNNGYTIERY IHGWEESYND IQPWKFVDVP
     STFGAKKDEY KTYQVRTRDE LRRLFGNEVF SSAPCLQLVE LYMPQEDAPA ALKSTAAAAA
     KSNAKA
//
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