ID ILVH_SYNY3 Reviewed; 172 AA. AC Q55141; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 138. DE RecName: Full=Acetolactate synthase small subunit; DE EC=2.2.1.6; DE AltName: Full=Acetohydroxy-acid synthase small subunit; DE Short=AHAS; DE Short=ALS; GN Name=ilvH; Synonyms=ilvN; OrderedLocusNames=sll0065; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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 -!- 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 -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA10276.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA10276.1; ALT_INIT; Genomic_DNA. DR PIR; S74358; S74358. DR AlphaFoldDB; Q55141; -. DR SMR; Q55141; -. DR IntAct; Q55141; 2. DR STRING; 1148.gene:10499775; -. DR PaxDb; 1148-1001135; -. DR EnsemblBacteria; BAA10276; BAA10276; BAA10276. DR KEGG; syn:sll0065; -. DR eggNOG; COG0440; Bacteria. DR InParanoid; Q55141; -. DR PhylomeDB; Q55141; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central. DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central. DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central. 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 1, CHLOROPLASTIC; 1. DR Pfam; PF13710; ACT_5; 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; Branched-chain amino acid biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..172 FT /note="Acetolactate synthase small subunit" FT /id="PRO_0000151418" FT DOMAIN 4..78 FT /note="ACT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007" SQ SEQUENCE 172 AA; 18871 MW; CF266998F9BCA806 CRC64; MKHTLSVLVE DEAGVLTRIA GLFARRGFNI ESLAVGSAEQ GDVSRITMVV PGDENTIEQL TKQLYKLVNV IKVQDITETP CVERELMLVK VSANAPNRAE VIELAQVFRA RIVDISEDTV TIEVVGDPGK MVAILQMLAK FGIKEVARTG KIALVRESGV NTEYLKSLES KF //