ID   PDC_NEUCR               Reviewed;         570 AA.
AC   P33287; Q7RV97; V5IKN9;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Pyruvate decarboxylase;
DE            EC=4.1.1.1;
DE   AltName: Full=8-10 nm cytoplasmic filament-associated protein;
DE   AltName: Full=P59NC;
DE   Flags: Precursor;
GN   Name=cfp; Synonyms=pdc-1; ORFNames=NCU02193;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 3-25.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=8359692; DOI=10.1016/0378-1119(93)90427-5;
RA   Alvarez M.E., Rosa A.L., Temporini E.D., Wolstenholme A., Panzetta G.,
RA   Patrito L., Maccioni H.J.F.;
RT   "The 59-kDa polypeptide constituent of 8-10-nm cytoplasmic filaments in
RT   Neurospora crassa is a pyruvate decarboxylase.";
RL   Gene 130:253-258(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mycelium;
RA   Temporini E.D., Alvarez M.E., Mautino M., Kawaguchi T., Kinghorn J.,
RA   Rosa A.L.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-25.
RX   PubMed=1352758; DOI=10.1093/genetics/131.3.575;
RA   Haedo S.D., Temporini E.D., Alvarez M.E., Maccioni H.J., Rosa A.L.;
RT   "Molecular cloning of a gene (cfp) encoding the cytoplasmic filament
RT   protein P59Nc and its genetic relationship to the snowflake locus of
RT   Neurospora crassa.";
RL   Genetics 131:575-580(1992).
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   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC       Note=Binds 1 metal ion per subunit.;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC       Note=Binds 1 thiamine pyrophosphate per subunit.;
CC   -!- PATHWAY: Carbohydrate metabolism; pyruvate metabolism.
CC   -!- SUBUNIT: Homomer.
CC   -!- INTERACTION:
CC       P33287; P33287: cfp; NbExp=5; IntAct=EBI-7533403, EBI-7533403;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Cytoplasmic filaments.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L09125; AAA33567.1; -; mRNA.
DR   EMBL; U65927; AAB17969.1; -; Genomic_DNA.
DR   EMBL; CM002242; ESA42032.1; -; Genomic_DNA.
DR   EMBL; S40298; AAB22524.2; -; mRNA.
DR   PIR; JN0782; JN0782.
DR   RefSeq; XP_011395109.1; XM_011396807.1.
DR   AlphaFoldDB; P33287; -.
DR   SMR; P33287; -.
DR   MINT; P33287; -.
DR   STRING; 5141.EFNCRP00000003234; -.
DR   EnsemblFungi; ESA42032; ESA42032; NCU02193.
DR   GeneID; 3875734; -.
DR   KEGG; ncr:NCU02193; -.
DR   VEuPathDB; FungiDB:NCU02193; -.
DR   InParanoid; P33287; -.
DR   OMA; IFWGQVS; -.
DR   UniPathway; UPA00231; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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   GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniPathway.
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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase; Magnesium;
KW   Metal-binding; Reference proteome; Thiamine pyrophosphate.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:8359692"
FT                   /id="PRO_0000035653"
FT   CHAIN           3..570
FT                   /note="Pyruvate decarboxylase"
FT                   /id="PRO_0000035654"
FT   REGION          394..476
FT                   /note="Thiamine pyrophosphate binding"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         477
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   570 AA;  62263 MW;  DF48B86C24EDAACF CRC64;
     MVAQQQGKFT VGDYLAERLA QVGVRHHFVV PGDYNLILLD KLQAHPDLKE VGCANELNCS
     LAAEGYARAN GISACVVTYS VGALSAFNGT GSAYAENLPL VLISGSPNTN DPSQYHILHH
     TLGHPDYTYQ YEMAKKITCC AVAIPRAIDA PRLIDRALRA AILARKPCYI EIPTNLAGAT
     CVRPGPISAI TDPITSDKSA LEAAAKCAAE YLDGKLKPVI LVGPKAGRAG SEKELIEFAE
     AMGCAVALQP AAKGMFPEDH KQFVGIFWGQ VSSDAADAMV HWADAMICVG AVFNDYSTVG
     WTAVPNIPLM TVDMDHVTFP GAHFSRVRMC EFLSHLATQV TFNDSTMIEY KRLKPDPPHV
     HTAEREEPLS RKEISRQVQE MLTDKTSLFV DTGDSWFNGI QLKLPPGAKF EIEMQWGHIG
     WSIPAAFGYA LRHPDRHTIV LVGDGSFQVT AQEVSQMVRF KVPITIMLIN NRGYTIEVEI
     HDGSYNKIKN WDYAMLVEAF NSTDGHAKGL LANTAGELAD AIKVAESHKE GPTLIECTID
     QDDCSKELIT WGHYVAAANA RPPRNMSVQE