ID   ILV6_SCHPO              Reviewed;         289 AA.
AC   O60086;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Probable acetolactate synthase small subunit;
DE   AltName: Full=Acetohydroxy-acid synthase small subunit;
DE            Short=AHAS;
DE            Short=ALS;
GN   ORFNames=SPBC14C8.04;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
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   -!- FUNCTION: Stimulates activity of the acetolactate synthase catalytic
CC       subunit ilv1. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA18422.2; -; Genomic_DNA.
DR   PIR; T39432; T39432.
DR   RefSeq; NP_595907.1; NM_001021815.2.
DR   AlphaFoldDB; O60086; -.
DR   SMR; O60086; -.
DR   STRING; 4896.SPBC14C8.04.1; -.
DR   iPTMnet; O60086; -.
DR   MaxQB; O60086; -.
DR   PaxDb; O60086; -.
DR   PRIDE; O60086; -.
DR   EnsemblFungi; SPBC14C8.04.1; SPBC14C8.04.1:pep; SPBC14C8.04.
DR   GeneID; 2540022; -.
DR   KEGG; spo:SPBC14C8.04; -.
DR   PomBase; SPBC14C8.04; -.
DR   VEuPathDB; FungiDB:SPBC14C8.04; -.
DR   eggNOG; KOG2663; Eukaryota.
DR   HOGENOM; CLU_055003_0_0_1; -.
DR   InParanoid; O60086; -.
DR   OMA; AHHREIT; -.
DR   PhylomeDB; O60086; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   PRO; PR:O60086; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005948; C:acetolactate synthase complex; ISO:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IBA:GO_Central.
DR   GO; GO:1990610; F:acetolactate synthase regulator activity; ISS:PomBase.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; ISO:PomBase.
DR   GO; GO:0009098; P:leucine biosynthetic process; ISO:PomBase.
DR   GO; GO:0009099; P:valine biosynthetic process; ISO:PomBase.
DR   CDD; cd04878; ACT_AHAS; 1.
DR   Gene3D; 3.30.70.1150; -; 1.
DR   InterPro; IPR004789; Acetalactate_synth_ssu.
DR   InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR   InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR039557; AHAS_ACT.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF10369; ALS_ss_C; 1.
DR   SUPFAM; SSF55021; SSF55021; 2.
DR   TIGRFAMs; TIGR00119; acolac_sm; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..289
FT                   /note="Probable acetolactate synthase small subunit"
FT                   /id="PRO_0000317338"
FT   DOMAIN          72..149
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   289 AA;  31834 MW;  538F65B7F0B4BA7B CRC64;
     MFARRCGRLA NRFVRLKSTS ATSPITYKAL HANSPLPRCR IIEPPRATVP EAVSNIIMST
     PFNRVQRPKR HVFNCLVQNE PGVLSRLSGI LAARGFNIDS LVVCATEVEN LSRMTIVLRG
     ADEVVEQAKR QIEDIVSVWA VLDYTGTSMV ERELLLAKVS LLGPDHFQEH FERSEKVAES
     TNAKAKSDGE GVMNANAALQ LRASQLAAIN QLTTLFHGRV ADISTETIIL ELTATPDRVD
     NFLSLLRPYG VLEACRTGTS AMTRAPHSNE VTEEAEDDVE VEEVFLPPG