ID   HOSM_YEAST              Reviewed;         440 AA.
AC   Q12122;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 83.
DE   RecName: Full=Homocitrate synthase, mitochondrial;
DE            EC=2.3.3.14;
DE   Flags: Precursor;
GN   Name=LYS21; OrderedLocusNames=YDL131W; ORFNames=D2195;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97127826; PubMed=8972577;
RX   DOI=10.1002/(SICI)1097-0061(199612)12:15<1549::AID-YEA42>3.3.CO;2-J;
RA   Woelfl S., Haneman V., Saluz H.P.;
RT   "Analysis of a 26,756 bp segment from the left arm of yeast chromosome
RT   IV.";
RL   Yeast 12:1549-1554(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND THR-410, AND
RP   MASS SPECTROMETRY.
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409 AND THR-410, AND
RP   MASS SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-332; THR-333;
RP   SER-409 AND THR-410, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + 2-oxoglutarate = (R)-2-
CC       hydroxybutane-1,2,4-tricarboxylate + CoA.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/4.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-8508, EBI-8508;
CC       P43582:-; NbExp=1; IntAct=EBI-8508, EBI-22766;
CC       P22696:ESS1; NbExp=1; IntAct=EBI-8508, EBI-6679;
CC       P48570:LYS20; NbExp=1; IntAct=EBI-8508, EBI-8502;
CC       P33203:PRP40; NbExp=1; IntAct=EBI-8508, EBI-701;
CC       P46995:SET2; NbExp=1; IntAct=EBI-8508, EBI-16985;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- MISCELLANEOUS: Present with 21900 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthetase/homocitrate
CC       synthase family.
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DR   EMBL; X96876; CAA65629.1; -; Genomic_DNA.
DR   EMBL; Z74179; CAA98700.1; -; Genomic_DNA.
DR   PIR; S67674; S67674.
DR   RefSeq; NP_010151.1; -.
DR   DIP; DIP:4634N; -.
DR   IntAct; Q12122; 16.
DR   PeptideAtlas; Q12122; -.
DR   PRIDE; Q12122; -.
DR   Ensembl; YDL131W; Saccharomyces cerevisiae.
DR   GeneID; 851425; -.
DR   GenomeReviews; Z71256_GR; YDL131W.
DR   KEGG; sce:YDL131W; -.
DR   NMPDR; fig|4932.3.peg.888; -.
DR   CYGD; YDL131w; -.
DR   SGD; S000002289; LYS21.
DR   HOGENOM; Q12122; -.
DR   OMA; Q12122; EITAMVE.
DR   BRENDA; 2.3.3.14; 250.
DR   NextBio; 968636; -.
DR   GermOnline; YDL131W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:EC.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic...; TAS:SGD.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011872; LysS_fun_arc.
DR   InterPro; IPR000891; PYR_CT.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR10277:SF8; LysS_fun_arc; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR02146; LysS_fung_arch; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis;
KW   Mitochondrion; Phosphoprotein; Transferase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    440       Homocitrate synthase, mitochondrial.
FT                                /FTId=PRO_0000001051.
FT   MOD_RES     217    217       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine.
FT   MOD_RES     333    333       Phosphothreonine.
FT   MOD_RES     409    409       Phosphoserine.
FT   MOD_RES     410    410       Phosphothreonine.
SQ   SEQUENCE   440 AA;  48594 MW;  6B01827D998FD9AD CRC64;
     MSENNEFQSV TESTTAPTTS NPYGPNPADY LSNVKNFQLI DSTLREGEQF ANAFFDTEKK
     IEIARALDDF GVDYIELTSP VASEQSRKDC EAICKLGLKA KILTHIRCHM DDARVAVETG
     VDGVDVVIGT SKFLRQYSHG KDMNYIAKSA VEVIEFVKSK GIEIRFSSED SFRSDLVDLL
     NIYKTVDKIG VNRVGIADTV GCANPRQVYE LIRTLKSVVS CDIECHFHND TGCAIANAYT
     ALEGGARLID VSVLGIGERN GITPLGGLMA RMIVAAPDYV RSKYKLHKIR DIENLVADAV
     EVNIPFNNPI TGFCAFTHKA GIHAKAILAN PSTYEILDPH DFGMKRYIHF ANRLTGWNAI
     KSRVDQLNLN LTDDQIKEVT AKIKKLGDVR PLNIDDVDSI IKDFHAELST PLLKPVNKGT
     DDDNIDISNG HVSKKAKVTK
//