Reviewed, UniProtKB/Swiss-Prot Q9RQ65 (ILVI_BUCSC)

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

Organism

Buchnera aphidicola subsp. Schlechtendalia chinensis

Taxonomic identifier

118110 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	574 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
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 – 574	574	Acetolactate synthase large subunit		PRO_0000090794
Regions
	Nucleotide binding	261 – 282	22	FAD By similarity
	Nucleotide binding	304 – 323	20	FAD By similarity
	Region	397 – 477	81	Thiamine pyrophosphate binding
Sites
	Metal binding	448	1	Magnesium By similarity
	Metal binding	475	1	Magnesium By similarity
	Binding site	51	1	Thiamine pyrophosphate By similarity
	Binding site	153	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RQ65-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: AE18D612C8CD32BD	FASTA	574	63,740
	10 20 30 40 50 60 MEMLSGSEMI IQSLIDQGIK YIFGYPGGAV LDIYDSLKST KKIKHILVRH EQGATHMADG 70 80 90 100 110 120 YARATGKIGV VLVTSGPGAT NSITGIATAY MDSIPIVVIS GQVSSSLIGY DAFQECDMIG 130 140 150 160 170 180 ISRPIVKHSF LVKKTEDIPI TFKKAFWLAS SGRPGPIVID LPKDILNSYN KKPYIWPIEV 190 200 210 220 230 240 NIRSYNPITK GHSRQIKKAI DILKLSKQPV IYAGGGVISA NCHNELKELA EKLNIPVTTS 250 260 270 280 290 300 LMALGAFPGN HPQNLQMLGM HGTYEANMAM HYADVILAIG VRFDDRTTNN VKKYCPNATI 310 320 330 340 350 360 IHIDIDPTSI SKTITAHIPI VGNAKNVLQQ ILVFINSNMF VKEFYCLKKW WIKIQSWKNK 370 380 390 400 410 420 NSLNFDTNSD NIKPQSVIKT IWKLTKGKAF ITSDVGQHQM FAALYYSFQK PRRWINSGGL 430 440 450 460 470 480 GTMGFGLPAA LGVKLAFPNE TVICVTGDGS IQMNIQELST AMQYELPILI LNLNNKSLGM 490 500 510 520 530 540 VKQWQDIIYS GRHSHSYMKS LPNFIKLAES YGHSGISINT PKELEKKLQL ALEKLQNGHL 550 560 570 VFVDIKIDAS EHVYPMQIRD GGMNNMLLRK NGQK

References

[1]	"Sequence evolution in bacterial endosymbionts having extreme base compositions." Clark M.A., Moran N.A., Baumann P. Mol. Biol. Evol. 16:1586-1598(1999) [PubMed: 10555290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF129502 Genomic DNA. Translation: AAF13791.1.
3D structure databases
HSSP	HSSP built from PDB template 1JSC based on UniProtKB P07342.
ModBase	Search...
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_BUCSC

Accession

Primary (citable) accession number: Q9RQ65

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 44 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)