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Database: UniProt
Entry: F8DI89_STREP
LinkDB: F8DI89_STREP
Original site: F8DI89_STREP 
ID   F8DI89_STREP            Unreviewed;       158 AA.
AC   F8DI89;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Acetolactate synthase small subunit {ECO:0000256|RuleBase:RU368092};
DE            Short=AHAS {ECO:0000256|RuleBase:RU368092};
DE            Short=ALS {ECO:0000256|RuleBase:RU368092};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU368092};
DE   AltName: Full=Acetohydroxy-acid synthase small subunit {ECO:0000256|RuleBase:RU368092};
GN   Name=ilvN {ECO:0000313|EMBL:AEH56948.1};
GN   OrderedLocusNames=HMPREF0833_11917 {ECO:0000313|EMBL:AEH56948.1};
OS   Streptococcus parasanguinis (strain ATCC 15912 / DSM 6778 / CIP 104372 /
OS   LMG 14537).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=760570 {ECO:0000313|EMBL:AEH56948.1, ECO:0000313|Proteomes:UP000001502};
RN   [1] {ECO:0000313|Proteomes:UP000001502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15912 / DSM 6778 / CIP 104372 / LMG 14537
RC   {ECO:0000313|Proteomes:UP000001502};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RT   "Complete sequence of Streptococcus parasanguinis strain ATCC 15912.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of 2 pyruvate molecules into
CC       acetolactate in the first common step of the biosynthetic pathway of
CC       the branched-amino acids such as leucine, isoleucine, and valine.
CC       {ECO:0000256|RuleBase:RU368092}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000673,
CC         ECO:0000256|RuleBase:RU368092};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU368092}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC       ECO:0000256|RuleBase:RU368092}.
CC   -!- SUBUNIT: Dimer of large and small chains.
CC       {ECO:0000256|ARBA:ARBA00011744, ECO:0000256|RuleBase:RU368092}.
CC   -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC       {ECO:0000256|ARBA:ARBA00006341, ECO:0000256|RuleBase:RU368092}.
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DR   EMBL; CP002843; AEH56948.1; -; Genomic_DNA.
DR   RefSeq; WP_003010242.1; NC_015678.1.
DR   AlphaFoldDB; F8DI89; -.
DR   GeneID; 75174791; -.
DR   KEGG; scp:HMPREF0833_11917; -.
DR   HOGENOM; CLU_055003_4_0_9; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000001502; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04878; ACT_AHAS; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.70.1150; ACT-like. Chain A, domain 2; 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   NCBIfam; TIGR00119; acolac_sm; 1.
DR   PANTHER; PTHR30239; ACETOLACTATE SYNTHASE SMALL SUBUNIT; 1.
DR   PANTHER; PTHR30239:SF0; ACETOLACTATE SYNTHASE SMALL SUBUNIT 2, CHLOROPLASTIC; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF10369; ALS_ss_C; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   PROSITE; PS51671; ACT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU368092};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU368092};
KW   Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:AEH56948.1}.
FT   DOMAIN          4..79
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   158 AA;  17591 MW;  C432D6FF2BE70364 CRC64;
     MRRMLTAKLQ NRSGVLNRFT GVLSRRQVNI ESISVGATEN PNVSRITIII DVASHDEVEQ
     IIKQLNRQVD VIRVRDITDK PHLEREVILV KVSAPAEKRA EILAIIQPFR ATVVDVAPSS
     ITVQMTGNAE KSEALIRVIR PYGIKNIART GATGFTRD
//
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