Reviewed, UniProtKB/Swiss-Prot Q6SSJ3 (ILVB_CRYNV)

Names and origin

Protein names

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

Gene names

Name:

ILV2

Organism

Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii)

Taxonomic identifier

178876 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length	718 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
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
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 718		Acetolactate synthase, mitochondrial		PRO_0000035662
Regions
	Nucleotide binding	397 – 418	22	FAD By similarity
	Nucleotide binding	449 – 468	20	FAD By similarity
	Region	541 – 621	81	Thiamine pyrophosphate binding
Sites
	Metal binding	592	1	Magnesium By similarity
	Metal binding	619	1	Magnesium By similarity
	Binding site	173	1	Thiamine pyrophosphate By similarity
	Binding site	275	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6SSJ3-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4A0B0F1F0BF7BAFD	FASTA	718	78,497
	10 20 30 40 50 60 MLTRQARLLR RIPPPNAVLQ SGLQRRHRST DRYSNNIHTS STQNAPAPVY DTPIREKGMT 70 80 90 100 110 120 LEAKERVRAH VRKIQSSAST AAASPAVRPQ PAQHFQAAPQ PMPTNMPRFE SDSQVKNGLD 130 140 150 160 170 180 YSFIGLSGGQ IFQEMMLRHD VKQVFGYPGG AILPVFDAIY NSPHFEFVLP RHEQGAGHMA 190 200 210 220 230 240 EGYARVSGKP GVVLVTSGPG ATNVITPMQD ALSDGVPMVV FCGQVATNLI GSDAFQEADV 250 260 270 280 290 300 VGISRSCTKW NVMVKDIAEL PRRINEAFKI ATTGRPGPVL VDLPKDVTAA ILRTPIPAKS 310 320 330 340 350 360 VQPGHSPYLP SNPLNPSSQP SDPLPGDADL ITEAAQMINK AKRPIIFAGN GVLSSPEGPK 370 380 390 400 410 420 LLKELSDKGR IPVTTTLQGL GAFDERDEKS LHMIGMHGSA YANFAMQEAD VLIALGVRFD 430 440 450 460 470 480 DRVTGKVDTF APAAKAAAAE GRGGIIHFEI QPKNINKIVE AQIPVLGDVV ASLGELVPQI 490 500 510 520 530 540 EAVDRSAWIG RCKATKERYP FTYTPSQEGQ KLKPQEVVQE LDRQAEALGK EKFVISTGVG 550 560 570 580 590 600 QHQMWACQYY RWTEPRSWVS SGGLGTMGFG LPSAIGAKVA APEKYVIDID GDASFSMTAM 610 620 630 640 650 660 ELATASQYDI GVKVLLFNNE FQGMVEQWQD LFYENRYSHT RMTNPDFVKL SESMGAKGLR 670 680 690 700 710 CTKLEDLPRM MKEFLEYDGK RPIVLECLVS SEHVYPMIPA GKALHEQLLH PLLRNGSE

References

[1]

"Cryptococcus neoformans Ilv2p confers resistance to sulfometuron methyl and is required for survival at 37 degrees C and in vivo." Kingsbury J.M., Yang Z., Ganous T.M., Cox G.M., McCusker J.H. Microbiology 150:1547-1558(2004) [PubMed: 15133116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY450850 Genomic DNA. Translation: AAR29084.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.2.1.6. 303268.
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_CRYNV

Accession

Primary (citable) accession number: Q6SSJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)