ID G9LQX8_PENCH Unreviewed; 571 AA.
AC G9LQX8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
GN ORFNames=EN45_020340 {ECO:0000313|EMBL:KZN91893.1};
OS Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076 {ECO:0000313|EMBL:AEW48429.1};
RN [1] {ECO:0000313|EMBL:AEW48429.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DS17690 {ECO:0000313|EMBL:AEW48429.1};
RA Daran J.-M.G., Veiga T., Solis Escalante D., Pronk J.T.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW48429.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DS17690 {ECO:0000313|EMBL:AEW48429.1};
RX PubMed=22158714; DOI=10.1128/EC.05285-11;
RA Veiga T., Solis-Escalante D., Romagnoli G., ten Pierick A., Hanemaaijer M.,
RA Deshmuhk A., Wahl A., Pronk J.T., Daran J.M.;
RT "Resolving phenylalanine metabolism sheds light on natural synthesis of
RT penicillin G in Penicillium chrysogenum.";
RL Eukaryot. Cell 11:238-249(2012).
RN [3] {ECO:0000313|EMBL:KZN91893.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P2niaD18 {ECO:0000313|EMBL:KZN91893.1};
RX PubMed=25059858; DOI=10.1128/genomeA.00577-14;
RA Specht T., Dahlmann T.A., Zadra I., Kurnsteiner H., Kuck U.;
RT "Complete sequencing and chromosome-scale genome assembly of the industrial
RT progenitor strain P2niaD18 from the penicillin producer Penicillium
RT chrysogenum.";
RL Genome Announc. 2:E0057714-E0057714(2014).
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; JQ086347; AEW48429.1; -; mRNA.
DR EMBL; CM002798; KZN91893.1; -; Genomic_DNA.
DR AlphaFoldDB; G9LQX8; -.
DR Proteomes; UP000076449; Chromosome i.
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 2: Evidence at transcript level;
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}; Pyruvate {ECO:0000313|EMBL:KZN91893.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..482
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 571 AA; 63357 MW; F511A6D03BEB394C CRC64;
MTQDIKLADY LFIRLRQLGV DSMFGVPGDY NLRLLDFVTP AGLHWVGNCN ELNAAYAADG
YGRIKGLSAL ITTYGVGELS AINGIAGAYA ENTPVLHIVG TPPRPLQSAR TFMHHTFSDG
DYRRFANMST HVTAAQARLE DATTAPERID YILRQALIHN RPVYLEFPDD MPDVLVSATN
LETKICIPQP PSSTQEPQVL ARILERVYSA KRPFIFVDGE STGLGIVDQL DALIKATNWP
TWTTVYGKGL VNEQLPNVYG LYAAAFGDKP AQEYFEQADL ILTFGPHNSD TNTYFYTTIP
KPAVAITFSG STVQIEHDTY RDLSARNILS KLLQSLDPAR LVKATGPPKQ ETTLANIQNT
DPIAQNNFYR LVNPLFREGD IILTETGTAA HGGRNFKLPA KSRIFGAVTW LSIGFMLPAT
LGTALAQREH NKGTESKSQT ILFIGDGSLQ MTAQEISVMI REKLNIIIFI INNDGYTIER
VIHGRKQVYN DVPFWRHAQA LNYFGADEEH AANNTFTART CGELKDVLAN ERIQNGSGVR
LVEVLMGRED VQGALLYLLN KQLDQEKETE Q
//
