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   03-AUG-2022, entry version 147.
DE   RecName: Full=Probable aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
GN   ORFNames=SPBC19F5.04;
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 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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND THR-328, 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=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC         Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5.
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA18652.1; -; Genomic_DNA.
DR   PIR; T39822; T39822.
DR   RefSeq; NP_596542.1; NM_001022463.2.
DR   AlphaFoldDB; O60163; -.
DR   SMR; O60163; -.
DR   BioGRID; 277128; 4.
DR   STRING; 4896.SPBC19F5.04.1; -.
DR   iPTMnet; O60163; -.
DR   SwissPalm; O60163; -.
DR   MaxQB; O60163; -.
DR   PaxDb; O60163; -.
DR   PRIDE; O60163; -.
DR   EnsemblFungi; SPBC19F5.04.1; SPBC19F5.04.1:pep; SPBC19F5.04.
DR   GeneID; 2540602; -.
DR   KEGG; spo:SPBC19F5.04; -.
DR   PomBase; SPBC19F5.04; -.
DR   VEuPathDB; FungiDB:SPBC19F5.04; -.
DR   eggNOG; KOG0456; Eukaryota.
DR   HOGENOM; CLU_009116_6_4_1; -.
DR   InParanoid; O60163; -.
DR   OMA; DMIVQTI; -.
DR   PhylomeDB; O60163; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   PRO; PR:O60163; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004072; F:aspartate kinase activity; ISO:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006531; P:aspartate metabolic process; IC:PomBase.
DR   GO; GO:0009090; P:homoserine biosynthetic process; ISO:PomBase.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
DR   GO; GO:0006555; P:methionine metabolic process; ISO:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; ISO:PomBase.
DR   CDD; cd04247; AAK_AK-Hom3; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041747; AK-Hom3.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55021; SSF55021; 2.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Threonine biosynthesis;
KW   Transferase.
FT   CHAIN           1..519
FT                   /note="Probable aspartokinase"
FT                   /id="PRO_0000066689"
FT   DOMAIN          363..435
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          436..510
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         328
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
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