ILVB_BACSU
ID ILVB_BACSU Reviewed; 574 AA.
AC P37251; P94564;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 146.
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;
DE AltName: Full=Vegetative protein 105;
DE Short=VEG105;
GN Name=ilvB; OrderedLocusNames=BSU28310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Vandeyar M.A., Vander Horn P.B., Rafael J.A., Grandoni J.A., Zahler S.A.;
RT "The ilv-leu operon of Bacillus subtilis: sequences of the ilvB, ilvN and
RT ilvC genes, and the control of transcription.";
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=1577690; DOI=10.1128/jb.174.10.3212-3219.1992;
RA Grandoni J.A., Zahler S.A., Calvo J.M.;
RT "Transcriptional regulation of the ilv-leu operon of Bacillus subtilis.";
RL J. Bacteriol. 174:3212-3219(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-15.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
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.
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; L03181; AAA22546.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99561.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14791.1; -; Genomic_DNA.
DR EMBL; M87009; AAA22550.1; -; Genomic_DNA.
DR PIR; B69644; B69644.
DR RefSeq; NP_390709.1; NC_000964.3.
DR RefSeq; WP_004398643.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P37251; -.
DR SMR; P37251; -.
DR STRING; 224308.BSU28310; -.
DR PaxDb; P37251; -.
DR PRIDE; P37251; -.
DR EnsemblBacteria; CAB14791; CAB14791; BSU_28310.
DR GeneID; 936792; -.
DR KEGG; bsu:BSU28310; -.
DR PATRIC; fig|224308.179.peg.3075; -.
DR eggNOG; COG0028; Bacteria.
DR InParanoid; P37251; -.
DR OMA; CFGTSGP; -.
DR PhylomeDB; P37251; -.
DR BioCyc; BSUB:BSU28310-MON; -.
DR BRENDA; 2.2.1.6; 658.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
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; 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.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Direct protein sequencing; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659"
FT CHAIN 2..574
FT /note="Acetolactate synthase large subunit"
FT /id="PRO_0000090786"
FT REGION 403..483
FT /note="Thiamine pyrophosphate binding"
FT BINDING 64
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 272..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 315..334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="A -> R (in Ref. 1; AAA22546)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..61
FT /note="NSGLVHILP -> IQVGTYPS (in Ref. 1; AAA22546)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..89
FT /note="KPGVVIATSG -> NRCRHCHVR (in Ref. 1; AAA22546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 62589 MW; 16B126E08A37859F CRC64;
MGTNVQVDSA SAECTQTMSG ALMLIESLKK EKVEMIFGYP GGAVLPIYDK LYNSGLVHIL
PRHEQGAIHA AEGYARVSGK PGVVIATSGP GATNLVTGLA DAMIDSLPLV VFTGQVATSV
IGSDAFQEAD ILGITMPVTK HSYQVRQPED LPRIIKEAFH IATTGRPGPV LIDIPKDVAT
IEGEFSYDHE MNLPGYQPTT EPNYLQIRKL VEAVSSAKKP VILAGAGVLH GKASEELKNY
AEQQQIPVAH TLLGLGGFPA DHPLFLGMAG MHGTYTANMA LHECDLLISI GARFDDRVTG
NLKHFARNAK IAHIDIDPAE IGKIMKTQIP VVGDSKIVLQ ELIKQDGKQS DSSEWKKQLA
EWKEEYPLWY VDNEEEGFKP QKLIEYIHQF TKGEAIVATD VGQHQMWSAQ FYPFQKADKW
VTSGGLGTMG FGLPAAIGAQ LAEKDATVVA VVGDGGFQMT LQELDVIREL NLPVKVVILN
NACLGMVRQW QEIFYEERYS ESKFASQPDF VKLSEAYGIK GIRISSEAEA KEKLEEALTS
REPVVIDVRV ASEEKVFPMV APGKGLHEMV GVKP
