PDC_ASPOR
ID PDC_ASPOR Reviewed; 570 AA.
AC Q2UKV4; O94185;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Pyruvate decarboxylase;
DE EC=4.1.1.1;
GN Name=pdcA; ORFNames=AO090003000661;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lee D.W., Koh J.S., Kim J.H., Chae K.-S.;
RT "Cloning and nucleotide sequence of one of the most highly expressed genes,
RT a pdcA homologue of Aspergillus nidulans, in Aspergillus oryzae.";
RL Biotechnol. Lett. 21:139-142(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526; Evidence={ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P06169};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD16178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF098293; AAD16178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP007155; BAE57811.1; -; Genomic_DNA.
DR RefSeq; XP_001819813.1; XM_001819761.2.
DR AlphaFoldDB; Q2UKV4; -.
DR SMR; Q2UKV4; -.
DR STRING; 510516.Q2UKV4; -.
DR PRIDE; Q2UKV4; -.
DR EnsemblFungi; BAE57811; BAE57811; AO090003000661.
DR GeneID; 5991796; -.
DR KEGG; aor:AO090003000661; -.
DR VEuPathDB; FungiDB:AO090003000661; -.
DR HOGENOM; CLU_013748_0_2_1; -.
DR OMA; EQRYNDI; -.
DR BRENDA; 4.1.1.43; 522.
DR Proteomes; UP000006564; Chromosome 2.
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 InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR012110; TPP_enzyme.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR43452; PTHR43452; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..570
FT /note="Pyruvate decarboxylase"
FT /id="PRO_0000233114"
FT BINDING 38
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 124
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 398
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 421..423
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 451..452
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 477..482
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 483
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
SQ SEQUENCE 570 AA; 62927 MW; 0B3464E3DD2516C3 CRC64;
MATDIATRDL RKPIDVAEYL FRRLREVGVR AVHGVPGDYN LVALDYLPKC DLHWVGNCNE
LNAGYAADGY ARINGMSALV TTFGVGELSA LNAIAGAYSE FVPIVHIVGQ PHTKSQKDGM
LLHHTLGNGD FNVFTRMSAD ISCTLGCLNS THEVATLIDN AIRECWIRSR PVYISLPTDM
VTKKIEGERL DTPLDLSLPP NDPEKEDYVV DVVLKYLHAA KKPVILVDAC AIRHRVLDEV
HEFVEKSGLP TFVAPMGKGA VDETHKNYGG VYAGTGSNPG VREQVESSDL ILSIGAIKSD
FNTTGFSYRI GQLNTIDFHS TYVRVRYSEY PDINMKGVLQ KIVQRMGNLN VGPVSPPSNL
LPDNEKASTE QAITHAWLWP TVGQWLKEKD VVITETGTAN FGIWDTRFPA GVTAISQVLW
GSIGYSVGAC QGAALAAKEQ GRRTVLFVGD GSFQLTLQEV STMIRNNLNP IIFVICNEGY
TIERYIHGWE AVYNDIQPWD FLNIPVAFGA KDKYKGYKVT TRDELRELFA NEEFASAPCL
QLVELHMPRD DCPASLKLTA ESAAERNKSL
