Reviewed, UniProtKB/Swiss-Prot O33112 (ILVB_MYCLE)

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:	ML1696
ORF Names:	MLCB637.20

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	625 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 – 625	625	Acetolactate synthase		PRO_0000090802
Regions
	Nucleotide binding	300 – 321	22	FAD By similarity
	Nucleotide binding	343 – 362	20	FAD By similarity
	Region	436 – 516	81	Thiamine pyrophosphate binding
Sites
	Metal binding	487	1	Magnesium By similarity
	Metal binding	514	1	Magnesium By similarity
	Binding site	92	1	Thiamine pyrophosphate By similarity
	Binding site	194	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O33112-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 53FBA3DA76A169D1	FASTA	625	67,021
	10 20 30 40 50 60 MSAPTKPHAR PQGAGNSVPN TVKPATQFPS KPAVAKLERV SPEQLTGAQS VIRSLEELDV 70 80 90 100 110 120 EVIFGIPGGA VLLVYDPLFY SKKLRHVLVR HEQGAGHAAS GYAHVTGKVG VCMATSGPGA 130 140 150 160 170 180 TNLVTPLADA QMDSVPVVAI TGQVGRSLIG TDAFQEADIS GITMPITKHN FLVRAGDDIP 190 200 210 220 230 240 RVLAEAFHIA SSGRPGAVLV DIPKDVLQGQ CKFSWPPKMD LPGYKPNTKP HNRQIRAAAK 250 260 270 280 290 300 LIADARKPVL YVGGGVIRGE ATEQLRDLAE LTGIPVVSTL MARGAFPDSH HQNLGMPGMH 310 320 330 340 350 360 GTVAAVAALQ RSDLLIALGT RFDDRVTGKL DSFAPDAKVI HADIDPAEIG KNRHADVPIV 370 380 390 400 410 420 GDVKAVIVEL IAMLRHYEVP GNIEMTDWWS YLDGVRKTYP LSYSPQSDGT LSPEYVIEKL 430 440 450 460 470 480 GEIVGPEAVY VAGVGQHQMW AAQFISYEKP RTWLNSGGLG TMGFAIPAAM GAKIARPEAE 490 500 510 520 530 540 VWAIDGDGCF QMTNQELATC AIEGAPIKVA LINNGNLGMV RQWQALFYQE RYSQTDLATH 550 560 570 580 590 600 SHRIPDFVKL AEALGCVGLR CECEEDVVDV INQARAINNR PVVIDFIVGA DAQVWPMVAA 610 620 GASNDEIQAA RGIRPLFDDE SEGHV

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z99263 Genomic DNA. Translation: CAB16435.1. AL583923 Genomic DNA. Translation: CAC30649.1.
PIR	T45413.
RefSeq	NP_302166.1.
3D structure databases
HSSP	HSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	910798.
GenomeReviews	Gene locus ML1696 in contig AL450380_GR.
KEGG	mle:ML1696.
NMPDR	fig|272631.1.peg.1038.
Organism-specific databases
Leproma	ML1696.
CMR	Search...
Phylogenomic databases
HOGENOM	O33112.
OMA	O33112. DIPRIVH.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1696-MON.
BRENDA	2.2.1.6. 808.
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_MYCLE

Accession

Primary (citable) accession number: O33112

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 66 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)