ILVX_BACSU
ID ILVX_BACSU Reviewed; 570 AA.
AC Q04789; O05225;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Acetolactate synthase;
DE EC=2.2.1.6;
DE AltName: Full=ALS;
DE AltName: Full=Acetohydroxy-acid synthase;
GN Name=alsS; OrderedLocusNames=BSU36010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7685336; DOI=10.1128/jb.175.12.3863-3875.1993;
RA Renna M.C., Najimudin N., Winik L.R., Zahler S.A.;
RT "Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in
RT post-exponential-phase production of acetoin.";
RL J. Bacteriol. 175:3863-3875(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
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 REGULATION.
RX PubMed=10809684; DOI=10.1128/jb.182.11.3072-3080.2000;
RA Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E.,
RA Dreesen O., Glaser P., Jahn D.;
RT "Fermentative metabolism of Bacillus subtilis: physiology and regulation of
RT gene expression.";
RL J. Bacteriol. 182:3072-3080(2000).
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: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC butane-2,3-diol from pyruvate: step 1/3.
CC -!- INDUCTION: Strongly induced under anaerobic conditions. Activated by
CC ResDE, Fnr and ArfM.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22222.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB07802.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L04470; AAA22222.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z93767; CAB07802.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15618.2; -; Genomic_DNA.
DR PIR; H69584; H69584.
DR RefSeq; NP_391482.2; NC_000964.3.
DR RefSeq; WP_003244057.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; Q04789; -.
DR SMR; Q04789; -.
DR STRING; 224308.BSU36010; -.
DR PaxDb; Q04789; -.
DR PRIDE; Q04789; -.
DR EnsemblBacteria; CAB15618; CAB15618; BSU_36010.
DR GeneID; 936852; -.
DR KEGG; bsu:BSU36010; -.
DR PATRIC; fig|224308.179.peg.3898; -.
DR eggNOG; COG0028; Bacteria.
DR InParanoid; Q04789; -.
DR OMA; DIGSHYI; -.
DR PhylomeDB; Q04789; -.
DR BioCyc; BSUB:BSU36010-MON; -.
DR BRENDA; 2.2.1.6; 658.
DR BRENDA; 4.1.1.72; 658.
DR UniPathway; UPA00626; UER00677.
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:0045151; P:acetoin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034077; P:butanediol metabolic process; 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 InterPro; IPR012782; Acetolactate_synth_catblc.
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; TIGR02418; acolac_catab; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 2: Evidence at transcript level;
KW Acetoin biosynthesis; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..570
FT /note="Acetolactate synthase"
FT /id="PRO_0000090799"
FT REGION 399..479
FT /note="Thiamine pyrophosphate binding"
FT BINDING 60
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 266..287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 308..327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 116
FT /note="D -> Y (in Ref. 1; AAA22222)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="A -> S (in Ref. 1; AAA22222)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="A -> H (in Ref. 1; AAA22222)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="G -> A (in Ref. 1; AAA22222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62004 MW; 47B7A64CE6C78EF7 CRC64;
MTKATKEQKS LVKNRGAELV VDCLVEQGVT HVFGIPGAKI DAVFDALQDK GPEIIVARHE
QNAAFMAQAV GRLTGKPGVV LVTSGPGASN LATGLLTANT EGDPVVALAG NVIRADRLKR
THQSLDNAAL FQPITKYSVE VQDVKNIPEA VTNAFRIASA GQAGAAFVSF PQDVVNEVTN
TKNVRAVAAP KLGPAADDAI SAAIAKIQTA KLPVVLVGMK GGRPEAIKAV RKLLKKVQLP
FVETYQAAGT LSRDLEDQYF GRIGLFRNQP GDLLLEQADV VLTIGYDPIE YDPKFWNING
DRTIIHLDEI IADIDHAYQP DLELIGDIPS TINHIEHDAV KVEFAEREQK ILSDLKQYMH
EGEQVPADWK SDRAHPLEIV KELRNAVDDH VTVTCDIGSH AIWMSRYFRS YEPLTLMISN
GMQTLGVALP WAIGASLVKP GEKVVSVSGD GGFLFSAMEL ETAVRLKAPI VHIVWNDSTY
DMVAFQQLKK YNRTSAVDFG NIDIVKYAES FGATGLRVES PDQLADVLRQ GMNAEGPVII
DVPVDYSDNI NLASDKLPKE FGELMKTKAL
