ID   AK_SCHPO                Reviewed;         519 AA.
AC   O60163;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Probable aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
GN   ORFNames=SPBC19F5.04;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-328, AND
RP   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: 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   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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DR   EMBL; CU329671; CAA18652.1; -; Genomic_DNA.
DR   PIR; T39822; T39822.
DR   RefSeq; NP_596542.1; -.
DR   GeneID; 2540602; -.
DR   KEGG; spo:SPBC19F5.04; -.
DR   NMPDR; fig|4896.1.peg.2408; -.
DR   GeneDB_Spombe; SPBC19F5.04; -.
DR   OMA; O60163; DITSTRM.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004539-MON; -.
DR   BRENDA; 2.7.2.4; 653.
DR   ArrayExpress; O60163; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW.
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; 1.
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    519       Probable aspartokinase.
FT                                /FTId=PRO_0000066689.
FT   DOMAIN      359    431       ACT 1.
FT   DOMAIN      435    503       ACT 2.
FT   MOD_RES     326    326       Phosphoserine.
FT   MOD_RES     328    328       Phosphothreonine.
SQ   SEQUENCE   519 AA;  56813 MW;  0B392EB4AE8ECFCB CRC64;
     MSIAKNIEND PSKGWVVQKF GGTSVGKFPI KIAVDVAKEY LSTKRVALVC SARSTDTKAE
     GTTTRLIRAT EAALRPAVGS VHDLVRIIET DHVQAARDFI QDVGIQDELI DAFHADCVEL
     EQYLNAIRVL SEVSPRTRDL VIGMGERLSC RFMAAVLKDQ GIDSEFIDMS HIIDEQREWR
     NLDASFYAYL ASQLASKVTA VGNKVPVVTG FFGMVPGGLL SQIGRGYTDF CAALLAVGLN
     ADELQIWKEV DGIFTADPRK VPTARLLPLI TPEEAAELTY YGSEVIHPFT MSQVVHARIP
     IRIKNVGNPR GKGTVIFPDT ISRHGSATPP HPPKIMPDDI SASLANKGAT AVTIKDTIMV
     INIQSNRKIS AHGFLASIFA ILDKYKLAVD LITTSEVHVS MALYEESDDG NMHEAFVELR
     RLGTLDILHG LAILSLVGKH MRNTTGYAGR MFCKLAEAQI NIEMISQGAS EINISCVIDE
     KMAVKALNVI HKELLEPLAL HEVPSQASML VEKPWLYSA
//