Reviewed, UniProtKB/Swiss-Prot Q04789 (ILVX_BACSU)

Names and origin

Protein names

Recommended name:
    Acetolactate synthase
    EC=2.2.1.6
Alternative name(s):
    Acetohydroxy-acid synthase
    ALS

Gene names

Name:	alsS
Ordered Locus Names:	BSU36010

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	2 pyruvate = 2-acetolactate + CO2.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Polyol metabolism; 2,3-butanediol biosynthesis; (R,R)-2,3-butanediol from pyruvate: step 1/3.
Induction	Strongly induced under anaerobic conditions. Activated by resDE, fnr and arfM.
Sequence similarities	Belongs to the TPP enzyme family.
Sequence caution	The sequence AAA22222.1 differs from that shown. Reason: Frameshift at position 64.

Ontologies

Keywords
Biological process	Acetoin biosynthesis
Ligand	FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acetoin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro acetolactate synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Acetolactate synthase		PRO_0000090799
Regions
	Nucleotide binding	266 – 287	22	FAD By similarity
	Nucleotide binding	308 – 327	20	FAD By similarity
	Region	399 – 479	81	Thiamine pyrophosphate binding
Sites
	Metal binding	450	1	Magnesium By similarity
	Binding site	60	1	Thiamine pyrophosphate By similarity
	Binding site	162	1	FAD By similarity
Experimental info
	Sequence conflict	116	1	D → Y in AAA22222. Ref.1
	Sequence conflict	401	1	A → S in AAA22222. Ref.1
	Sequence conflict	484	1	A → H in AAA22222. Ref.1
	Sequence conflict	515	1	G → A in AAA22222. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q04789-1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 47B7A64CE6C78EF7	FASTA	570	62,004
	10 20 30 40 50 60 MTKATKEQKS LVKNRGAELV VDCLVEQGVT HVFGIPGAKI DAVFDALQDK GPEIIVARHE 70 80 90 100 110 120 QNAAFMAQAV GRLTGKPGVV LVTSGPGASN LATGLLTANT EGDPVVALAG NVIRADRLKR 130 140 150 160 170 180 THQSLDNAAL FQPITKYSVE VQDVKNIPEA VTNAFRIASA GQAGAAFVSF PQDVVNEVTN 190 200 210 220 230 240 TKNVRAVAAP KLGPAADDAI SAAIAKIQTA KLPVVLVGMK GGRPEAIKAV RKLLKKVQLP 250 260 270 280 290 300 FVETYQAAGT LSRDLEDQYF GRIGLFRNQP GDLLLEQADV VLTIGYDPIE YDPKFWNING 310 320 330 340 350 360 DRTIIHLDEI IADIDHAYQP DLELIGDIPS TINHIEHDAV KVEFAEREQK ILSDLKQYMH 370 380 390 400 410 420 EGEQVPADWK SDRAHPLEIV KELRNAVDDH VTVTCDIGSH AIWMSRYFRS YEPLTLMISN 430 440 450 460 470 480 GMQTLGVALP WAIGASLVKP GEKVVSVSGD GGFLFSAMEL ETAVRLKAPI VHIVWNDSTY 490 500 510 520 530 540 DMVAFQQLKK YNRTSAVDFG NIDIVKYAES FGATGLRVES PDQLADVLRQ GMNAEGPVII 550 560 570 DVPVDYSDNI NLASDKLPKE FGELMKTKAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin." Renna M.C., Najimudin N., Winik L.R., Zahler S.A. J. Bacteriol. 175:3863-3875(1993) [PubMed: 7685336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed: 9353933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Fermentative metabolism of Bacillus subtilis: physiology and regulation of gene expression." Cruz Ramos H., Hoffmann T., Marino M., Nedjari H., Presecan-Siedel E., Dreesen O., Glaser P., Jahn D. J. Bacteriol. 182:3072-3080(2000) [PubMed: 10809684] [Abstract] Cited for: REGULATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L04470 Genomic DNA. Translation: AAA22222.1. Frameshift. Z93767 Genomic DNA. Translation: CAB07802.1. Different initiation. AL009126 Genomic DNA. Translation: CAB15618.2.
PIR	H69584.
RefSeq	NP_391482.1.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	936852.
GenomeReviews	Gene locus BSU36010 in contig AL009126_GR.
KEGG	bsu:BSU36010.
NMPDR	fig|224308.1.peg.3608.
Organism-specific databases
SubtiList	BG10471. alsS. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	Q04789.
OMA	Q04789. VSFPQDV.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3599-MON.
BRENDA	2.2.1.6. 150.
Family and domain databases
InterPro	IPR012782. Acetolactate_synth_catblc. IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view]
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR02418. acolac_catab. 1 hit.
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVX_BACSU

Accession

Primary (citable) accession number: Q04789
Secondary accession number(s): O05225

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)