PDC_EMENI
ID PDC_EMENI Reviewed; 568 AA.
AC P87208; C8V9T0; Q5B3J2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Pyruvate decarboxylase;
DE EC=4.1.1.1;
GN Name=pdcA; ORFNames=AN4888;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9210590; DOI=10.1016/s0378-1119(97)00032-2;
RA Lockington R.A., Borlace G.N., Kelly J.M.;
RT "Pyruvate decarboxylase and anaerobic survival in Aspergillus nidulans.";
RL Gene 191:61-67(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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=AAB63012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA60966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U73194; AAB63012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AACD01000084; EAA60966.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001303; CBF76546.1; -; Genomic_DNA.
DR RefSeq; XP_662492.1; XM_657400.1.
DR AlphaFoldDB; P87208; -.
DR SMR; P87208; -.
DR STRING; 162425.CADANIAP00005515; -.
DR PRIDE; P87208; -.
DR EnsemblFungi; CBF76546; CBF76546; ANIA_04888.
DR EnsemblFungi; EAA60966; EAA60966; AN4888.2.
DR GeneID; 2872690; -.
DR KEGG; ani:AN4888.2; -.
DR VEuPathDB; FungiDB:AN4888; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; P87208; -.
DR OMA; EQRYNDI; -.
DR OrthoDB; 560466at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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..568
FT /note="Pyruvate decarboxylase"
FT /id="PRO_0000090763"
FT BINDING 37
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 123
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 397
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 420..422
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"
FT CONFLICT 8..9
FT /note="EL -> DV (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="A -> R (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..218
FT /note="VDVVLKYLHA -> LVDARAQVFARS (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..235
FT /note="ACAIRHRV -> DSCVFDDSTGLS (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> T (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..413
FT /note="WDTRFPSGVTA -> CWNLLPSELQP (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="N -> G (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="A -> T (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
FT CONFLICT 542..568
FT /note="LVEVHMPREDAPASLKITAEAAASRNK -> VSLCDLTHYLSDANFEQLG
FT (in Ref. 1; AAB63012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 62599 MW; A5EE862F15D6A36C CRC64;
MADIATRELR QPIDIAEYLF RRLHEVGIRS VHGVPGDYNL AALDYLPKCG LHWVGNCNEL
NAGYAADGYA RVNGIAALVT TFGVGELSAI NAIAGAYSEF VPIIHIVGQP HSRSQKDGLL
LHHTLGNGDY NVFSSMNKGI SVTTANLNDT YDAATLIDNA IRECWIHSRP VYLALPTDMI
TKKIEGERLK TPIDLSLPAN DPEKEDYVVD VVLKYLHAAK NPVILVDACA IRHRVLEEVH
DLIEVSGLPT FVAPMGKGAV NETHRCYGGV YAGTGSNPGV REQVESSDLI LSIGAIKSDF
NTAGFSYRIG QLNTIDFHST YVRVRYSEYP DTNMKGVLRK VIQRLGFIKA DPVPHISNAL
PEHEKNSSEQ RITHAWMWPM VGQWLKENDI VITETGTANF GIWDTRFPSG VTAISQVLWG
SIGYSVGACQ GAALAAKEQG NRRTVLWVGD GSLQLTLQEI STMIRNNLNP IIFVICNEGY
TIERFIHGWD ESYNDIQTWD IKGLPVAFGG KGRYKGYKVT TRDELTKLFA SEEFSSAPCL
QLVEVHMPRE DAPASLKITA EAAASRNK
