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Database: UniProt
Entry: D7E722_METEZ
LinkDB: D7E722_METEZ
Original site: D7E722_METEZ 
ID   D7E722_METEZ            Unreviewed;       161 AA.
AC   D7E722;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   OrderedLocusNames=Metev_0745 {ECO:0000313|EMBL:ADI73646.1};
OS   Methanohalobium evestigatum (strain ATCC BAA-1072 / DSM 3721 / NBRC 107634
OS   / OCM 161 / Z-7303).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalobium.
OX   NCBI_TaxID=644295 {ECO:0000313|EMBL:ADI73646.1, ECO:0000313|Proteomes:UP000000391};
RN   [1] {ECO:0000313|EMBL:ADI73646.1, ECO:0000313|Proteomes:UP000000391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1072 / DSM 3721 / NBRC 107634 / OCM 161 / Z-7303
RC   {ECO:0000313|Proteomes:UP000000391};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence chromosome of Methanohalobium evestigatum Z-7303.";
RL   Submitted (JUN-2010) 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|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|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; CP002069; ADI73646.1; -; Genomic_DNA.
DR   RefSeq; WP_013194214.1; NC_014253.1.
DR   AlphaFoldDB; D7E722; -.
DR   STRING; 644295.Metev_0745; -.
DR   GeneID; 9346366; -.
DR   KEGG; mev:Metev_0745; -.
DR   HOGENOM; CLU_055003_1_3_2; -.
DR   OrthoDB; 85792at2157; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000000391; Chromosome.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000000391};
KW   Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:ADI73646.1}.
FT   DOMAIN          4..78
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   161 AA;  17944 MW;  9AFCAA9C81B9E09D CRC64;
     MKHTLAVLVE NKYGVLARVA GLFSRRGYNI DSLAVGITDD PDISRMSIVV HGDDHVLEQV
     TKQLNKLVDV IRVTDLDAKD SVERELALIK VTTDTKTRPE IMQIVDVFRA RTVDVAAKSM
     TIEITGNEDK INAIEQLLRP FGIKEMVRTG KIAMTRGIKK S
//
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