ID   AK_YEAST                Reviewed;         527 AA.
AC   P10869;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   16-JUN-2009, entry version 84.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
GN   Name=HOM3; OrderedLocusNames=YER052C;
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].
RX   MEDLINE=88115350; PubMed=2892836;
RA   Rafalski J.A., Falco S.C.;
RT   "Structure of the yeast HOM3 gene which encodes aspartokinase.";
RL   J. Biol. Chem. 263:2146-2151(1988).
RN   [2]
RP   SEQUENCE REVISION.
RX   MEDLINE=90368723; PubMed=2168408;
RA   Rafalski J.A., Falco S.C.;
RT   "Structure of the yeast HOM3 gene which encodes aspartokinase.";
RL   J. Biol. Chem. 265:15346-15346(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313264; PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND MASS
RP   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333 AND SER-441, AND
RP   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: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC   -!- INTERACTION:
CC       P20081:FPR1; NbExp=1; IntAct=EBI-2430, EBI-6961;
CC   -!- MISCELLANEOUS: Present with 48100 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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DR   EMBL; J03526; AAA34681.1; -; Genomic_DNA.
DR   EMBL; U18796; AAB64587.1; -; Genomic_DNA.
DR   PIR; A35888; KIBYD.
DR   RefSeq; NP_010972.1; -.
DR   DIP; DIP:1319N; -.
DR   IntAct; P10869; 13.
DR   PeptideAtlas; P10869; -.
DR   PRIDE; P10869; -.
DR   Ensembl; YER052C; Saccharomyces cerevisiae.
DR   GeneID; 856778; -.
DR   GenomeReviews; U00092_GR; YER052C.
DR   KEGG; sce:YER052C; -.
DR   NMPDR; fig|4932.3.peg.2035; -.
DR   CYGD; YER052c; -.
DR   SGD; S000000854; HOM3.
DR   HOGENOM; P10869; -.
DR   OMA; P10869; KLSCLFM.
DR   BRENDA; 2.7.2.4; 250.
DR   NextBio; 982982; -.
DR   ArrayExpress; P10869; -.
DR   GermOnline; YER052C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006555; P:methionine metabolic process; TAS:SGD.
DR   GO; GO:0042493; P:response to drug; IMP:SGD.
DR   GO; GO:0009088; P:threonine biosynthetic process; IDA:SGD.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kin_reg.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 2.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN         1    527       Aspartokinase.
FT                                /FTId=PRO_0000066690.
FT   DOMAIN      363    433       ACT 1.
FT   DOMAIN      438    506       ACT 2.
FT   MOD_RES     333    333       Phosphothreonine.
FT   MOD_RES     441    441       Phosphoserine.
SQ   SEQUENCE   527 AA;  58110 MW;  D4D28FB8D4374898 CRC64;
     MPMDFQPTSS HSNWVVQKFG GTSVGKFPVQ IVDDIVKHYS KPDGPNNNVA VVCSARSSYT
     KAEGTTSRLL KCCDLASQES EFQDIIEVIR QDHIDNADRF ILNPALQAKL VDDTNKELEL
     VKKYLNASKV LGEVSSRTVD LVMSCGEKLS CLFMTALCND RGCKAKYVDL SHIVPSDFSA
     SALDNSFYTF LVQALKEKLA PFVSAKERIV PVFTGFFGLV PTGLLNGVGR GYTDLCAALI
     AVAVNADELQ VWKEVDGIFT ADPRKVPEAR LLDSVTPEEA SELTYYGSEV IHPFTMEQVI
     RAKIPIRIKN VQNPLGNGTI IYPDNVAKKG ESTPPHPPEN LSSSFYEKRK RGATAITTKN
     DIFVINIHSN KKTLSHGFLA QIFTILDKYK LVVDLISTSE VHVSMALPIP DADSLKSLRQ
     AEEKLRILGS VDITKKLSIV SLVGKHMKQY IGIAGTMFTT LAEEGINIEM ISQGANEINI
     SCVINESDSI KALQCIHAKL LSERTNTSNQ FEHAIDERLE QLKRLGI
//