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Database: UniProt
Entry: K0J7Q5_AMPXN
LinkDB: K0J7Q5_AMPXN
Original site: K0J7Q5_AMPXN 
ID   K0J7Q5_AMPXN            Unreviewed;       174 AA.
AC   K0J7Q5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
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=ilvN {ECO:0000313|EMBL:BAM47778.1};
GN   OrderedLocusNames=AXY_16460 {ECO:0000313|EMBL:BAM47778.1};
OS   Amphibacillus xylanus (strain ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667
OS   / NBRC 15112 / Ep01).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX   NCBI_TaxID=698758 {ECO:0000313|EMBL:BAM47778.1, ECO:0000313|Proteomes:UP000006294};
RN   [1] {ECO:0000313|EMBL:BAM47778.1, ECO:0000313|Proteomes:UP000006294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51415 / DSM 6626 / JCM 7361 / LMG 17667 / NBRC 15112 /
RC   Ep01 {ECO:0000313|Proteomes:UP000006294};
RA   Nakazawa H., Katano Y., Nakamura S., Sasagawa M., Fukada J., Arai T.,
RA   Sasakura N., Mochizuki D., Hosoyama A., Harada K., Horikawa H., Kato Y.,
RA   Harada T., Sasaki K., Sekiguchi M., Hodoyama M., Nishiko R., Narita H.,
RA   Hanamaki A., Hata C., Konno Y., Niimura Y., Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Amphibacillus xylinus NBRC 15112.";
RL   Submitted (JAN-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; AP012050; BAM47778.1; -; Genomic_DNA.
DR   RefSeq; WP_015010372.1; NC_018704.1.
DR   AlphaFoldDB; K0J7Q5; -.
DR   STRING; 698758.AXY_16460; -.
DR   KEGG; axl:AXY_16460; -.
DR   PATRIC; fig|698758.3.peg.1642; -.
DR   eggNOG; COG0440; Bacteria.
DR   HOGENOM; CLU_055003_4_0_9; -.
DR   OrthoDB; 9787365at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000006294; 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:UP000006294};
KW   Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:BAM47778.1}.
FT   DOMAIN          4..79
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   174 AA;  19452 MW;  9401A9723E1704D1 CRC64;
     MKRIITAKVR NRSGVLNRIT GLLQKRQFNI ESISVGRTEQ EGISRITFVV DVEDFPKAEQ
     ITKQLNKQID VLKVTDITDK AIVARELALI KITSNAQMRS EIQGLIDPFR ATVIDVSKDT
     ISVQVTGDTE KVEALIELLK PYGIKDLART GITAFLRGHQ PQANPDQEPF SLLN
//
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