ID A0A173XX75_9FIRM Unreviewed; 165 AA.
AC A0A173XX75;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ilvH_2 {ECO:0000313|EMBL:CUN55185.1};
GN Synonyms=ilvN {ECO:0000313|EMBL:RYT65236.1};
GN ORFNames=EAI82_12145 {ECO:0000313|EMBL:RYT65236.1}, ERS852394_00444
GN {ECO:0000313|EMBL:CUN55185.1}, ROSSTS7063_02834
GN {ECO:0000313|EMBL:VUX18439.1};
OS Blautia obeum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=40520 {ECO:0000313|EMBL:CUN55185.1, ECO:0000313|Proteomes:UP000095409};
RN [1] {ECO:0000313|EMBL:CUN55185.1, ECO:0000313|Proteomes:UP000095409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUN55185.1,
RC ECO:0000313|Proteomes:UP000095409};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RYT65236.1, ECO:0000313|Proteomes:UP000293506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=af_0058 {ECO:0000313|Proteomes:UP000293506}, and Af_0058
RC {ECO:0000313|EMBL:RYT65236.1};
RX PubMed=30630933; DOI=.1126/science.aau5238;
RA Jiang X., Hall A.B., Arthur T.D., Plichta D.R., Covington C.T., Poyet M.,
RA Crothers J., Moses P.L., Tolonen A.C., Vlamakis H., Alm E.J., Xavier R.J.;
RT "Invertible promoters mediate bacterial phase variation, antibiotic
RT resistance, and host adaptation in the gut.";
RL Science 363:181-187(2019).
RN [3] {ECO:0000313|EMBL:VUX18439.1, ECO:0000313|Proteomes:UP000409147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ruminococcus_obeum_SSTS_Bg7063 {ECO:0000313|EMBL:VUX18439.1};
RA Hibberd C M., Gehrig L. J., Chang H.-W., Venkatesh S.;
RL Submitted (JUL-2019) 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}.
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; CYZD01000002; CUN55185.1; -; Genomic_DNA.
DR EMBL; RCXQ01000012; RYT65236.1; -; Genomic_DNA.
DR EMBL; CABHNB010000043; VUX18439.1; -; Genomic_DNA.
DR RefSeq; WP_055065555.1; NZ_WWVS01000012.1.
DR AlphaFoldDB; A0A173XX75; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000095409; Unassembled WGS sequence.
DR Proteomes; UP000293506; Unassembled WGS sequence.
DR Proteomes; UP000409147; Unassembled WGS sequence.
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 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 {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 Reference proteome {ECO:0000313|Proteomes:UP000095409};
KW Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:CUN55185.1}.
FT DOMAIN 5..79
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 165 AA; 18038 MW; 350A18ED8B6864F1 CRC64;
MHKRILSLLV DNTAGVLSRI SGLFSRRGYN IDSLTVGVTA DERYSRMTVV CSGDSMILEQ
ITKQLAKLVD VRDIKVLEPD NSVSRELVLV KVAARPEQRE GIISIANIFR ANVIDVGKTS
LVIEMTGSKS KLGAFIDLLG EYEILELART GITGLSRGAS DVKFL
//