Reviewed, UniProtKB/Swiss-Prot O85293 (ILVI_BUCAP)

Names and origin

Protein names

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

Gene names

Name:	ilvI
Ordered Locus Names:	BUsg_220

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	571 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.
Subunit structure	Dimer of large and small chains By similarity.
Miscellaneous	Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry By similarity.
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 – 571	571	Acetolactate synthase large subunit		PRO_0000090792
Regions
	Nucleotide binding	261 – 282	22	FAD By similarity
	Nucleotide binding	304 – 323	20	FAD By similarity
	Region	394 – 474	81	Thiamine pyrophosphate binding
Sites
	Metal binding	445	1	Magnesium By similarity
	Metal binding	472	1	Magnesium By similarity
	Binding site	51	1	Thiamine pyrophosphate By similarity
	Binding site	153	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	O85293-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: DF8D20AC282BE6DB	FASTA	571	63,267
	10 20 30 40 50 60 MEILSGAEMV IRSLINQGIQ HIFGYPGGAV LDIYDALKTV GGVEHILVRH EQAATHMADG 70 80 90 100 110 120 YARSTGKIGV VLVTSGPGAT NAITGIATAY MDSIPMVVIS GQVASSLIGY DAFQECDMIG 130 140 150 160 170 180 ISRPIVKHSF LVKRTEDIPI IFKKAFWLAS TGRPGPVVID LPKDILKKTN KYNFIWPKNI 190 200 210 220 230 240 HIRSYNPTTK GHQGQIKKAL RILLKAKKPI IYAGGGIISS NSSEELRIFA EKINCPVTTS 250 260 270 280 290 300 LMGLGAFPGN HIQSISMLGM HGTYEANMAM HYSDVIFAIG VRFDDRTTNN LKKYCPNATI 310 320 330 340 350 360 LHVDIDPTSI SKTVSADIPI VGDAKQVLKE MIELIKKEKQ IHSLKEWWSS IGKWKKIKSL 370 380 390 400 410 420 EYNKKSNKIK PQKIIQTLFK LTKGTSYITS DVGQHQMFTA LYYQFNKPRR WINSGGLGTM 430 440 450 460 470 480 GFGLPAALGV KLALPKATVI CVTGDGSIQM NIQELSTARQ YNLAVLILNL NNSSLGMVKQ 490 500 510 520 530 540 WQDMIYSGRH SHSYMDSLPD FVKLVESYGH IGLKVKTNEE LEEKLILALK KLSEGNLVFL 550 560 570 DIQIDDSEHV YPMQIQGGGM NEMWLRKKEV S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of a DNA fragment from Buchnera aphidicola (Aphid endosymbiont) containing the genes dapD-htrA-ilvI-ilvH-ftsL-ftsI-murE." Thao M.L., Baumann P. Curr. Microbiol. 37:214-216(1998) [PubMed: 9688822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF060492 Genomic DNA. Translation: AAC32333.1. AE013218 Genomic DNA. Translation: AAM67780.1.
RefSeq	NP_660569.1.
3D structure databases
HSSP	HSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	1005419.
GenomeReviews	Gene locus BUsg_220 in contig AE013218_GR.
KEGG	bas:BUsg220.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O85293.
OMA	O85293. ECDMIGI.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG220-MON.
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

ILVI_BUCAP

Accession

Primary (citable) accession number: O85293

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 65 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)