ID E6Q9N0_9ZZZZ Unreviewed; 163 AA.
AC E6Q9N0;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetolactate synthase isozyme III small subunit (AHAS-III) (Acetohydroxy-acid synthase III small subunit) (ALS-III) {ECO:0000313|EMBL:CBI03906.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CBI03906.1};
GN Name=ilvH {ECO:0000313|EMBL:CBI03906.1};
GN ORFNames=CARN5_2670 {ECO:0000313|EMBL:CBI03906.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI03906.1};
RN [1] {ECO:0000313|EMBL:CBI03906.1}
RP NUCLEOTIDE SEQUENCE.
RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA Le Paslier D.;
RT "Diversity of trophic interactions inside an arsenic-rich microbial
RT ecosystem.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000256|ARBA:ARBA00006341}.
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:CBI03906.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABP01000033; CBI03906.1; -; Genomic_DNA.
DR AlphaFoldDB; E6Q9N0; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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 Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Transferase {ECO:0000313|EMBL:CBI03906.1}.
FT DOMAIN 6..80
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 163 AA; 17998 MW; 5EB12D5C09013110 CRC64;
MTMRHIISIL LENEAGALSR VAGLFSARGY NIEAMTVAPT HDPSISRMTV ATRGSEEIME
QVLKQLNKLV EVVRVHDLTE GPHIERELML VKVHAMGPDR EEVKRLSDIF RGRIIDVTDR
SYTMELTGTG EKLDAFIQSL DPGMVIEVVR SGASAISRGA KAI
//