Reviewed, UniProtKB/Swiss-Prot P57321 (ILVI_BUCAI)

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:	BU226

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [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_0000090791
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)
	P57321-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 493E32351D21FC48	FASTA	571	63,176
	10 20 30 40 50 60 MEILSGAEMV VRSLIDQGIQ HIFGYPGGAV LDIYDALKTV GGIEHILVRH EQAATHMADG 70 80 90 100 110 120 YSRSTGKTGV VLVTSGPGAT NAITGIATAY MDSIPMVVIS GQVASSLIGY DAFQECDMIG 130 140 150 160 170 180 ISRPIVKHSF LVKKTEDIPI VFKKAFWLAS SGRPGPIVID LPKDILKKDN KYLYKWPDNI 190 200 210 220 230 240 NIRSYNPTTK GHIGQIKKAL HTLLKAQRPV IYAGGGIISS NSSEELRIFA EKINCPVTTS 250 260 270 280 290 300 LMGLGSFPGT HDQNISMLGM HGTYEANMTM HHADVIFAIG VRFDDRTTNN LNKYCPNAIV 310 320 330 340 350 360 LHVDIDPTSI SKTVSANIPI VGDAKHVLQK MIELLKKEKK ISLLEDWWNT IKKWKKINSL 370 380 390 400 410 420 QYNQLSNKIK PQTVIKTLFK LTKGTSYITS DVGQHQMFTA LYYPFNKPRR WINSGGLGTM 430 440 450 460 470 480 GFGLPAALGV KLALPKETVI CITGDGSIQM NIQELSTARQ YNLAVLILNL NNSSLGMVKQ 490 500 510 520 530 540 WQDMIYSGRH SHSYMDSLPD FVKLSESYGH FGIQITEPIE LEEKLMLALS KLSDGHLVFV 550 560 570 DVQIDNSEHV YPMQIQGGGM NEMRLRKKEV A

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB12942.1.
RefSeq	NP_240056.1.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	1109669.
GenomeReviews	Gene locus BU226 in contig BA000003_GR.
KEGG	buc:BU226.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57321.
OMA	P57321. ECDMIGI.
Enzyme and pathway databases
BioCyc	BSP107806:BU226-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_BUCAI

Accession

Primary (citable) accession number: P57321

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 54 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)