ID G5IH08_9CLOT Unreviewed; 166 AA.
AC G5IH08;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=HMPREF9473_02786 {ECO:0000313|EMBL:EHI59229.1};
OS Hungatella hathewayi WAL-18680.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI59229.1, ECO:0000313|Proteomes:UP000005384};
RN [1] {ECO:0000313|EMBL:EHI59229.1, ECO:0000313|Proteomes:UP000005384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI59229.1,
RC ECO:0000313|Proteomes:UP000005384};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL Submitted (AUG-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHI59229.1}.
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DR EMBL; ADLN01000070; EHI59229.1; -; Genomic_DNA.
DR RefSeq; WP_006780765.1; NZ_JH379027.1.
DR AlphaFoldDB; G5IH08; -.
DR PATRIC; fig|742737.3.peg.2793; -.
DR HOGENOM; CLU_055003_1_3_9; -.
DR OrthoDB; 9787365at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000005384; 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; 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:UP000005384};
KW Transferase {ECO:0000256|RuleBase:RU368092}.
FT DOMAIN 5..79
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 166 AA; 18562 MW; D6FB34F0AD81EB89 CRC64;
MDRIVLSLLV DNTAGVLSRV AGLFSRRGYN IESLTVGVTA DERYSRMTVV SFGDQNILEQ
IEKQLRKLED VRDIKKLEPG RSVYRELIMV KVRANASERQ AVSAISDIFR ATIVDVGKDS
LTVMLTGDQS KLDALVNLLE DYEILELART GLTGLERGSD DIRYLP
//
