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PRPD_YEAST
ID   PRPD_YEAST              Reviewed;         516 AA.
AC   Q12428; D6W413;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Probable 2-methylcitrate dehydratase {ECO:0000250|UniProtKB:P77243};
DE            Short=2-MC dehydratase {ECO:0000250|UniProtKB:P77243};
DE            EC=4.2.1.79 {ECO:0000250|UniProtKB:P77243};
DE   AltName: Full=(2S,3S)-2-methylcitrate dehydratase {ECO:0000250|UniProtKB:P77243};
GN   Name=PDH1; OrderedLocusNames=YPR002W; ORFNames=LPZ2W, YP9723.02;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Catalyzes the stereospecific dehydration of (2S,3S)-2-
CC       methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate.
CC       {ECO:0000250|UniProtKB:P77243}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-2-methylcitrate = 2-methyl-cis-aconitate + H2O;
CC         Xref=Rhea:RHEA:17725, ChEBI:CHEBI:15377, ChEBI:CHEBI:57872,
CC         ChEBI:CHEBI:58853; EC=4.2.1.79;
CC         Evidence={ECO:0000250|UniProtKB:P77243};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000250|UniProtKB:P77243}.
CC   -!- MISCELLANEOUS: Present with 2730 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PrpD family. {ECO:0000305}.
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DR   EMBL; Z71255; CAA95042.1; -; Genomic_DNA.
DR   EMBL; Z48951; CAA88780.1; -; Genomic_DNA.
DR   EMBL; U31900; AAA97581.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11429.1; -; Genomic_DNA.
DR   PIR; S52815; S52815.
DR   RefSeq; NP_015326.1; NM_001184099.1.
DR   AlphaFoldDB; Q12428; -.
DR   SMR; Q12428; -.
DR   BioGRID; 36178; 34.
DR   IntAct; Q12428; 2.
DR   MINT; Q12428; -.
DR   STRING; 4932.YPR002W; -.
DR   MaxQB; Q12428; -.
DR   PaxDb; Q12428; -.
DR   PRIDE; Q12428; -.
DR   EnsemblFungi; YPR002W_mRNA; YPR002W; YPR002W.
DR   GeneID; 856108; -.
DR   KEGG; sce:YPR002W; -.
DR   SGD; S000006206; PDH1.
DR   VEuPathDB; FungiDB:YPR002W; -.
DR   eggNOG; ENOG502QPZI; Eukaryota.
DR   GeneTree; ENSGT00390000015700; -.
DR   HOGENOM; CLU_021803_1_0_1; -.
DR   InParanoid; Q12428; -.
DR   OMA; ECTKHLG; -.
DR   BioCyc; YEAST:G3O-34164-MON; -.
DR   UniPathway; UPA00946; -.
DR   PRO; PR:Q12428; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q12428; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0047547; F:2-methylcitrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019541; P:propionate metabolic process; IMP:SGD.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 1.10.4100.10; -; 1.
DR   Gene3D; 3.30.1330.120; -; 1.
DR   InterPro; IPR012705; 2Me_IsoCit_deHydtase_PrpD.
DR   InterPro; IPR036148; MmgE/PrpD_sf.
DR   InterPro; IPR042183; MmgE/PrpD_sf_1.
DR   InterPro; IPR042188; MmgE/PrpD_sf_2.
DR   InterPro; IPR005656; MmgE_PrpD.
DR   InterPro; IPR045337; MmgE_PrpD_C.
DR   InterPro; IPR045336; MmgE_PrpD_N.
DR   PANTHER; PTHR16943; PTHR16943; 1.
DR   Pfam; PF03972; MmgE_PrpD; 1.
DR   Pfam; PF19305; MmgE_PrpD_C; 1.
DR   SUPFAM; SSF103378; SSF103378; 1.
DR   TIGRFAMs; TIGR02330; prpD; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..516
FT                   /note="Probable 2-methylcitrate dehydratase"
FT                   /id="PRO_0000215027"
SQ   SEQUENCE   516 AA;  57684 MW;  2ED7F1AF648F2AAC CRC64;
     MFLAKNLKNN KIKVCLPKKK FAALSTASIQ TNERPNPDKV LKDIAKYVHE TPLKSSLALD
     TARLCFLDTL GCGLAALKFK QAQNIIKPIV PGTIVPSGTK ILGTSYVMDP VKGAFAIGTL
     IRWLDYNDCW LAAEWGHPSD NLGGILAVAD HLSRLNKATH GKNGKQFLVK DVLEAMIKAH
     EIQGIIALEN SFNKVGLDHV VLVKVATAGV VSKMLGLSQE QTIEALSQAF VDGQSLRTYR
     HAPNTGSRKS WAAGDAVSRA VNLAYLVKNA NVGTIPSVLT ARTWGFYDVL FKGKPFSFQQ
     RSKYDSYVME NVLFKISFPA EFHAQTAVEA AVKAYRILAK QGKTFKDIKS IRIRTQEAAM
     RIIDKSGPLY NYADRDHCIQ YMIAVPLITG NLTATDYSDE VARNPEIDNL RSKMYCIEDT
     HLTQNYHDPD KRSIGNALLI ELNDGTQLDE IFVEYPVGHK FRREEGIPLL MNKFQRHLRE
     HFVESPDKVD LIMKVSSKTN FLNMQIDKYM DLFTEG
 
 
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