PDC3_SCHPO
ID PDC3_SCHPO Reviewed; 572 AA.
AC Q9P7P6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable pyruvate decarboxylase C186.09;
DE EC=4.1.1.1;
GN ORFNames=SPAC186.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; CU329670; CAB75873.1; -; Genomic_DNA.
DR PIR; T50136; T50136.
DR RefSeq; NP_595027.1; NM_001020457.1.
DR AlphaFoldDB; Q9P7P6; -.
DR SMR; Q9P7P6; -.
DR BioGRID; 279056; 16.
DR STRING; 4896.SPAC186.09.1; -.
DR PaxDb; Q9P7P6; -.
DR EnsemblFungi; SPAC186.09.1; SPAC186.09.1:pep; SPAC186.09.
DR GeneID; 2542602; -.
DR KEGG; spo:SPAC186.09; -.
DR PomBase; SPAC186.09; -.
DR VEuPathDB; FungiDB:SPAC186.09; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q9P7P6; -.
DR OMA; VYWYARH; -.
DR PhylomeDB; Q9P7P6; -.
DR PRO; PR:Q9P7P6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; ISM:PomBase.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:PomBase.
DR GO; GO:0006090; P:pyruvate metabolic process; ISM:PomBase.
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 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..572
FT /note="Probable pyruvate decarboxylase C186.09"
FT /id="PRO_0000090769"
FT REGION 400..482
FT /note="Thiamine pyrophosphate binding"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 483
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 572 AA; 62615 MW; B2985DDEE7F4E257 CRC64;
MKDNQQAVQL QQPTTIGHYL AVRLAQAGVK HHFVVPGDYN LGLLDKLQYN NYLEEVNCAN
ELNCAFAAEG YARANGIAAC VVTYSVGAFT AFDGIGGAYA EDLPVILISG SPNTNDIGSS
HLLHHTLGTH DFSYQYEMAK KITCAAVSIQ RPTEAPRLID YAIKMALLKK KPVYIEVPTN
VASQPCAAPG PASLITEPET SNQEYLQMAV DISAKIVNGK QKPVLLAGPK LRSFKAESAF
LELANSLNCS VAVMPNAKSF FPESHPNYAG IYWGQASTLG AESIINWSDC IICAGTTFTD
YSSNGWTSLP PKANVLHVDV DRVTVSDAEF GGVLLRDFLH ELAKKVKANN ASVVEYKRIR
PESLEIPMEN PKAALNRKEI IRQVQNLVNQ ETTLFVDTGD SWFGGMRITL PEKARFEIEM
QWGHIGWSVP SAFGYAIGAP KRNVVVFVGD GSFQETVQEV SQMVRLNLPI IMFLINNRGY
TIEVEIHDGP YNRIKNWDYA AIVEAFNAGE GHAKGFRVGN GHELAEAIRQ AKENSQGPTL
IECNIDQDDC SKELINWGHN VGAANGKPPA KE