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Database: UniProt
Entry: A0A099I7S4_CLOIN
LinkDB: A0A099I7S4_CLOIN
Original site: A0A099I7S4_CLOIN 
ID   A0A099I7S4_CLOIN        Unreviewed;       170 AA.
AC   A0A099I7S4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 48.
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:MZH61456.1};
GN   ORFNames=ADH65_16840 {ECO:0000313|EMBL:ASU21083.1}, CIAN88_05580
GN   {ECO:0000313|EMBL:KGJ54019.1}, GT649_16015
GN   {ECO:0000313|EMBL:MZH61456.1}, I5Q87_12050
GN   {ECO:0000313|EMBL:QQR24662.1};
OS   Clostridium innocuum.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=1522 {ECO:0000313|EMBL:KGJ54019.1, ECO:0000313|Proteomes:UP000030008};
RN   [1] {ECO:0000313|EMBL:KGJ54019.1, ECO:0000313|Proteomes:UP000030008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AN88 {ECO:0000313|EMBL:KGJ54019.1,
RC   ECO:0000313|Proteomes:UP000030008};
RA   Feng Y., Chiu C.-H.;
RT   "Clostridium innocuum, an unnegligible vancomycin-resistant pathogen
RT   causing extra-intestinal infections.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ASU21083.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I46 {ECO:0000313|EMBL:ASU21083.1};
RX   PubMed=29051233;
RA   Garzetti D., Brugiroux S., Bunk B., Pukall R., McCoy K.D., Macpherson A.J.,
RA   Stecher B.;
RT   "High-Quality Whole-Genome Sequences of the Oligo-Mouse-Microbiota
RT   Bacterial Community.";
RL   Genome Announc. 5:e00758-17(2017).
RN   [3] {ECO:0000313|Proteomes:UP000214713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I46 {ECO:0000313|Proteomes:UP000214713};
RA   Garzetti D.;
RT   "High-quality whole genome sequences of the Oligo-Mouse-Microbiota.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:MZH61456.1, ECO:0000313|Proteomes:UP000478871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A13 {ECO:0000313|EMBL:MZH61456.1,
RC   ECO:0000313|Proteomes:UP000478871};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
RN   [5] {ECO:0000313|EMBL:QQR24662.1, ECO:0000313|Proteomes:UP000595712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I46 {ECO:0000313|EMBL:QQR24662.1,
RC   ECO:0000313|Proteomes:UP000595712};
RA   Marbouty M., Lamy-Besnier Q., Debarbieux L., Koszul R.;
RT   "Closed and high quality bacterial genomes of the OMM12 community.";
RL   Submitted (NOV-2020) 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; CP022722; ASU21083.1; -; Genomic_DNA.
DR   EMBL; JQIF01000023; KGJ54019.1; -; Genomic_DNA.
DR   EMBL; WWTM01000035; MZH61456.1; -; Genomic_DNA.
DR   EMBL; CP065320; QQR24662.1; -; Genomic_DNA.
DR   RefSeq; WP_002606390.1; NZ_WWTY01000034.1.
DR   GeneID; 61928217; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000030008; Unassembled WGS sequence.
DR   Proteomes; UP000214713; Chromosome.
DR   Proteomes; UP000478871; Unassembled WGS sequence.
DR   Proteomes; UP000595712; 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   Transferase {ECO:0000256|RuleBase:RU368092, ECO:0000313|EMBL:MZH61456.1}.
FT   DOMAIN          10..84
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   170 AA;  19359 MW;  9CFF095DAC349488 CRC64;
     MNGNGMKKRW ISLYVENQVG VLSKISGLFS GKSYNLDSLT VGTTEDPTIS RMTIATVSDD
     ETFEQIKKQL NRLVEVIKVI DFTDIFVRMK EILYVKVQNC TLQEKTELFQ IAQTFKAKVI
     DYGRDSLLLE FVQTATKNDA VIKLMKEEFR DIEVVRGGSV GIESISMMER
//
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