ILV6_YEAST
ID ILV6_YEAST Reviewed; 309 AA.
AC P25605; D6VR03; P87009;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Acetolactate synthase small subunit, mitochondrial;
DE AltName: Full=Acetohydroxy-acid synthase small subunit;
DE Short=AHAS;
DE Short=ALS;
DE Flags: Precursor;
GN Name=ILV6; OrderedLocusNames=YCL009C; ORFNames=YCL9C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION TO 300.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SIMILARITY TO ACETOLACTATE SYNTHASE SMALL SUBUNITS.
RX PubMed=1304897; DOI=10.1002/pro.5560011216;
RA Bork P., Ouzounis C., Sander C., Scharf M., Schneider R., Sonnhammer E.;
RT "Comprehensive sequence analysis of the 182 predicted open reading frames
RT of yeast chromosome III.";
RL Protein Sci. 1:1677-1690(1992).
RN [5]
RP PROTEIN SEQUENCE OF 25-44.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483834; DOI=10.1002/yea.320110702;
RA Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P.,
RA Perrot M.;
RT "Two-dimensional protein map of Saccharomyces cerevisiae: construction of a
RT gene-protein index.";
RL Yeast 11:601-613(1995).
RN [6]
RP FUNCTION.
RX PubMed=8972574;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1511::aid-yea41>3.0.co;2-b;
RA Cullin C., Baudin-Baillieu A., Guillemet E., Ozier-Kalogeropoulos O.;
RT "Functional analysis of YCL09C: evidence for a role as the regulatory
RT subunit of acetolactate synthase.";
RL Yeast 12:1511-1518(1996).
RN [7]
RP FUNCTION, SUBUNIT, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=10213630; DOI=10.1021/bi983013m;
RA Pang S.S., Duggleby R.G.;
RT "Expression, purification, characterization, and reconstitution of the
RT large and small subunits of yeast acetohydroxyacid synthase.";
RL Biochemistry 38:5222-5231(1999).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Regulatory subunit of mitochondrial acetolactate synthase,
CC which catalyzes the first of a series of common steps in the
CC biosynthesis of the branched-chain amino acids. Stimulates activity of
CC the acetolactate synthase catalytic subunit ILV2 seven- to tenfold and
CC confers sensitivity to inhibition by valine and activation by ATP.
CC {ECO:0000269|PubMed:10213630, ECO:0000269|PubMed:8972574}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000305|PubMed:10213630}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000305|PubMed:10213630}.
CC -!- SUBUNIT: The acetolactate synthase complex contains the catalytic
CC regulatory subunit ILV2 and the regulatory small subunit ILV6.
CC {ECO:0000269|PubMed:10213630}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10213630}.
CC -!- MISCELLANEOUS: Present with 15800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000305}.
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DR EMBL; X59720; CAA42350.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07472.1; -; Genomic_DNA.
DR PIR; S19411; S19411.
DR RefSeq; NP_009918.1; NM_001178658.1.
DR PDB; 6U9D; X-ray; 3.19 A; C/D/G/H/K/L/O/P/S/T/W/X=41-309.
DR PDB; 6WO1; X-ray; 3.30 A; B=1-309.
DR PDBsum; 6U9D; -.
DR PDBsum; 6WO1; -.
DR AlphaFoldDB; P25605; -.
DR SMR; P25605; -.
DR BioGRID; 30972; 117.
DR ComplexPortal; CPX-3034; Acetolactate synthase complex.
DR DIP; DIP-671N; -.
DR IntAct; P25605; 18.
DR MINT; P25605; -.
DR STRING; 4932.YCL009C; -.
DR iPTMnet; P25605; -.
DR MaxQB; P25605; -.
DR PaxDb; P25605; -.
DR PRIDE; P25605; -.
DR EnsemblFungi; YCL009C_mRNA; YCL009C; YCL009C.
DR GeneID; 850348; -.
DR KEGG; sce:YCL009C; -.
DR SGD; S000000515; ILV6.
DR VEuPathDB; FungiDB:YCL009C; -.
DR eggNOG; KOG2663; Eukaryota.
DR HOGENOM; CLU_055003_0_0_1; -.
DR InParanoid; P25605; -.
DR OMA; AHHREIT; -.
DR BioCyc; YEAST:YCL009C-MON; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR PRO; PR:P25605; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25605; protein.
DR GO; GO:0005948; C:acetolactate synthase complex; IDA:SGD.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:SGD.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Direct protein sequencing;
KW Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7483834"
FT CHAIN 25..309
FT /note="Acetolactate synthase small subunit, mitochondrial"
FT /id="PRO_0000015637"
FT DOMAIN 79..159
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6WO1"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 211..229
FT /evidence="ECO:0007829|PDB:6U9D"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:6U9D"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:6U9D"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:6WO1"
FT TURN 286..290
FT /evidence="ECO:0007829|PDB:6U9D"
SQ SEQUENCE 309 AA; 33987 MW; BF36073D89BC0065 CRC64;
MLRSLLQSGH RRVVASSCAT MVRCSSSSTS ALAYKQMHRH ATRPPLPTLD TPSWNANSAV
SSIIYETPAP SRQPRKQHVL NCLVQNEPGV LSRVSGTLAA RGFNIDSLVV CNTEVKDLSR
MTIVLQGQDG VVEQARRQIE DLVPVYAVLD YTNSEIIKRE LVMARISLLG TEYFEDLLLH
HHTSTNAGAA DSQELVAEIR EKQFHPANLP ASEVLRLKHE HLNDITNLTN NFGGRVVDIS
ETSCIVELSA KPTRISAFLK LVEPFGVLEC ARSGMMALPR TPLKTSTEEA ADEDEKISEI
VDISQLPPG
