PDC2_SCHPO
ID PDC2_SCHPO Reviewed; 569 AA.
AC Q92345; P78913;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable pyruvate decarboxylase C1F8.07c;
DE EC=4.1.1.1;
GN ORFNames=SPAC1F8.07c;
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 MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
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).
RN [3]
RP IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=972 / ATCC 24843, and JY3;
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; THR-521 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB03601.3; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D89264; BAA13925.1; -; mRNA.
DR EMBL; CU329670; CAB03601.3; ALT_FRAME; Genomic_DNA.
DR PIR; T38114; T38114.
DR PIR; T43191; T43191.
DR RefSeq; NP_592796.3; NM_001018196.3.
DR AlphaFoldDB; Q92345; -.
DR SMR; Q92345; -.
DR IntAct; Q92345; 5.
DR MINT; Q92345; -.
DR STRING; 4896.SPAC1F8.07c.1; -.
DR iPTMnet; Q92345; -.
DR MaxQB; Q92345; -.
DR PaxDb; Q92345; -.
DR PRIDE; Q92345; -.
DR GeneID; 2541874; -.
DR KEGG; spo:SPAC1F8.07c; -.
DR PomBase; SPAC1F8.07c; -.
DR eggNOG; KOG1184; Eukaryota.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q92345; -.
DR PRO; PR:Q92345; -.
DR Proteomes; UP000002485; Chromosome I.
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; 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 1: Evidence at protein level;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..569
FT /note="Probable pyruvate decarboxylase C1F8.07c"
FT /id="PRO_0000090768"
FT REGION 396..478
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 446
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 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 182
FT /note="P -> A (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> T (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="A -> G (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="P -> S (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="A -> T (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="P -> S (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
FT CONFLICT 540..569
FT /note="AIDTDDCTQELVDWGKAVRSANARPPTADN -> PIDEAACIQEWIAGYRTF
FT TPRKIQLTFLDTQACMAAGLLSASEGTPYSES (in Ref. 1; BAA13925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 61719 MW; 8853F3C9BDB644D1 CRC64;
MTKDAESTMT VGTYLAQRLV EIGIKNHFVV PGDYNLRLLD FLEYYPGLSE IGCCNELNCA
FAAEGYARSN GIACAVVTYS VGALTAFDGI GGAYAENLPV ILVSGSPNTN DLSSGHLLHH
TLGTHDFEYQ MEIAKKLTCA AVAIKRAEDA PVMIDHAIRQ AILQHKPVYI EIPTNMANQP
CPVPGPISAV ISPEISDKES LEKATDIAAE LISKKEKPIL LAGPKLRAAG AESAFVKLAE
ALNCAAFIMP AAKGFYSEEH KNYAGVYWGE VSSSETTKAV YESSDLVIGA GVLFNDYSTV
GWRAAPNPNI LLNSDYTSVS IPGYVFSRVY MAEFLELLAK KVSKKPATLE AYNKARPQTV
VPKAAEPKAA LNRVEVMRQI QGLVDSNTTL YAETGDSWFN GLQMKLPAGA KFEVEMQWGH
IGWSVPSAMG YAVAAPERRT IVMVGDGSFQ LTGQEISQMI RHKLPVLIFL LNNRGYTIEI
QIHDGPYNRI QNWDFAAFCE SLNGETGKAK GLHAKTGEEL TSAIKVALQN KEGPTLIECA
IDTDDCTQEL VDWGKAVRSA NARPPTADN
