ILVI_BUCAP
ID ILVI_BUCAP Reviewed; 571 AA.
AC O85293;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Acetolactate synthase large subunit;
DE Short=AHAS;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase large subunit;
DE Short=ALS;
GN Name=ilvI; OrderedLocusNames=BUsg_220;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9688822; DOI=10.1007/s002849900365;
RA Thao M.L., Baumann P.;
RT "Sequence analysis of a DNA fragment from Buchnera aphidicola (Aphid
RT endosymbiont) containing the genes dapD-htrA-ilvI-ilvH-ftsL-ftsI-murE.";
RL Curr. Microbiol. 37:214-216(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4.
CC -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}.
CC -!- MISCELLANEOUS: Contains 1 molecule of FAD per monomer. The role of this
CC cofactor is not clear considering that the reaction does not involve
CC redox chemistry (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AF060492; AAC32333.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67780.1; -; Genomic_DNA.
DR RefSeq; WP_011053747.1; NC_004061.1.
DR AlphaFoldDB; O85293; -.
DR SMR; O85293; -.
DR STRING; 198804.BUsg_220; -.
DR PRIDE; O85293; -.
DR EnsemblBacteria; AAM67780; AAM67780; BUsg_220.
DR KEGG; bas:BUsg_220; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 391134at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; 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; cd02015; TPP_AHAS; 1.
DR InterPro; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR00118; acolac_lg; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; FAD;
KW Flavoprotein; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW Transferase.
FT CHAIN 1..571
FT /note="Acetolactate synthase large subunit"
FT /id="PRO_0000090792"
FT REGION 394..474
FT /note="Thiamine pyrophosphate binding"
FT BINDING 51
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 261..282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 304..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 571 AA; 63267 MW; DF8D20AC282BE6DB CRC64;
MEILSGAEMV IRSLINQGIQ HIFGYPGGAV LDIYDALKTV GGVEHILVRH EQAATHMADG
YARSTGKIGV VLVTSGPGAT NAITGIATAY MDSIPMVVIS GQVASSLIGY DAFQECDMIG
ISRPIVKHSF LVKRTEDIPI IFKKAFWLAS TGRPGPVVID LPKDILKKTN KYNFIWPKNI
HIRSYNPTTK GHQGQIKKAL RILLKAKKPI IYAGGGIISS NSSEELRIFA EKINCPVTTS
LMGLGAFPGN HIQSISMLGM HGTYEANMAM HYSDVIFAIG VRFDDRTTNN LKKYCPNATI
LHVDIDPTSI SKTVSADIPI VGDAKQVLKE MIELIKKEKQ IHSLKEWWSS IGKWKKIKSL
EYNKKSNKIK PQKIIQTLFK LTKGTSYITS DVGQHQMFTA LYYQFNKPRR WINSGGLGTM
GFGLPAALGV KLALPKATVI CVTGDGSIQM NIQELSTARQ YNLAVLILNL NNSSLGMVKQ
WQDMIYSGRH SHSYMDSLPD FVKLVESYGH IGLKVKTNEE LEEKLILALK KLSEGNLVFL
DIQIDDSEHV YPMQIQGGGM NEMWLRKKEV S
