ID F0T2P7_SYNGF Unreviewed; 159 AA.
AC F0T2P7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=Sgly_2157 {ECO:0000313|EMBL:ADY56446.1};
OS Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Syntrophobotulus.
OX NCBI_TaxID=645991 {ECO:0000313|EMBL:ADY56446.1, ECO:0000313|Proteomes:UP000007488};
RN [1] {ECO:0000313|EMBL:ADY56446.1, ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RX PubMed=21886864;
RA Han C., Mwirichia R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Syntrophobotulus glycolicus type strain
RT (FlGlyR).";
RL Stand. Genomic Sci. 4:371-380(2011).
RN [2] {ECO:0000313|Proteomes:UP000007488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8271 / FlGlyR {ECO:0000313|Proteomes:UP000007488};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
RA Chertkov O., Held B., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Syntrophobotulus glycolicus DSM 8271.";
RL Submitted (FEB-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; CP002547; ADY56446.1; -; Genomic_DNA.
DR RefSeq; WP_013625313.1; NC_015172.1.
DR AlphaFoldDB; F0T2P7; -.
DR STRING; 645991.Sgly_2157; -.
DR KEGG; sgy:Sgly_2157; -.
DR eggNOG; COG0440; Bacteria.
DR HOGENOM; CLU_055003_1_3_9; -.
DR OrthoDB; 9787365at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000007488; 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; 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:UP000007488};
KW Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:ADY56446.1}.
FT DOMAIN 4..78
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 159 AA; 17853 MW; E7AA8783FE0A8DBB CRC64;
MLHTLAVLVE NNPGVLARVS GLFARRAYNI YSLTVSQTEN PALSLMTIVV EGDGQVIEQV
TKQLHKLIVV HKVTNLSNEN VVERELALIR VKVRTETRLE VLQLVDVFRG RVVDMGKNSI
MIEMTGDIDK IDAFIKTLRP FGIQELVRTG KISVMRSEN
//
