Reviewed, UniProtKB/Swiss-Prot P0A623 (ILVB_MYCBO)

Names and origin

Protein names

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

Gene names

Name:	ilvB
Ordered Locus Names:	Mb3028c

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	618 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid 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 – 618	618	Acetolactate synthase		PRO_0000090801
Regions
	Nucleotide binding	293 – 314	22	FAD By similarity
	Nucleotide binding	336 – 355	20	FAD By similarity
	Region	429 – 509	81	Thiamine pyrophosphate binding
Sites
	Metal binding	480	1	Magnesium By similarity
	Metal binding	507	1	Magnesium By similarity
	Binding site	85	1	Thiamine pyrophosphate By similarity
	Binding site	187	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A623-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 9E0523F4AD6EC6AF	FASTA	618	66,123
	10 20 30 40 50 60 MSAPTKPHSP TFKPEPHSAA NEPKHPAARP KHVALQQLTG AQAVIRSLEE LGVDVIFGIP 70 80 90 100 110 120 GGAVLPVYDP LFDSKKLRHV LVRHEQGAGH AASGYAHVTG RVGVCMATSG PGATNLVTPL 130 140 150 160 170 180 ADAQMDSIPV VAITGQVGRG LIGTDAFQEA DISGITMPIT KHNFLVRSGD DIPRVLAEAF 190 200 210 220 230 240 HIAASGRPGA VLVDIPKDVL QGQCTFSWPP RMELPGYKPN TKPHSRQVRE AAKLIAAARK 250 260 270 280 290 300 PVLYVGGGVI RGEATEQLRE LAELTGIPVV TTLMARGAFP DSHRQNLGMP GMHGTVAAVA 310 320 330 340 350 360 ALQRSDLLIA LGTRFDDRVT GKLDSFAPEA KVIHADIDPA EIGKNRHADV PIVGDVKAVI 370 380 390 400 410 420 TELIAMLRHH HIPGTIEMAD WWAYLNGVRK TYPLSYGPQS DGSLSPEYVI EKLGEIAGPD 430 440 450 460 470 480 AVFVAGVGQH QMWAAQFIRY EKPRSWLNSG GLGTMGFAIP AAMGAKIALP GTEVWAIDGD 490 500 510 520 530 540 GCFQMTNQEL ATCAVEGIPV KVALINNGNL GMVRQWQSLF YAERYSQTDL ATHSHRIPDF 550 560 570 580 590 600 VKLAEALGCV GLRCEREEDV VDVINQARAI NDCPVVIDFI VGADAQVWPM VAAGTSNDEI 610 QAARGIRPLF DDITEGHA

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX248344 Genomic DNA. Translation: CAD96715.1.
RefSeq	NP_856673.1.
3D structure databases
HSSP	HSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	1093674.
GenomeReviews	Gene locus Mb3028c in contig BX248333_GR.
KEGG	mbo:Mb3028c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A623.
OMA	P0A623. HSWRYDH.
Enzyme and pathway databases
BRENDA	2.2.1.6. 3091.
Family and domain databases
InterPro	IPR012846. Acetolactate_synth_lsu. 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	TIGR00118. acolac_lg. 1 hit.
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVB_MYCBO

Accession

Primary (citable) accession number: P0A623
Secondary accession number(s): O53250

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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