P36620 (ILVB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetolactate synthase, mitochondrial
EC=2.2.1.6

Alternative name(s):
AHAS
ALS
Acetohydroxy-acid synthase

Gene names

Name:	ilv1
ORF Names:	SPBP35G2.07

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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.
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from genetic interaction. Source: GeneDB_Spombe
Cellular component	acetolactate synthase complex Inferred from sequence or structural similarity. Source: GeneDB_Spombe mitochondrion Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	acetolactate synthase activity Inferred from genetic interaction. Source: GeneDB_Spombe flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro thiamine 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 – 140	140	Mitochondrion Potential
	Chain	141 – 669	529	Acetolactate synthase, mitochondrial		PRO_0000035663
Regions
	Nucleotide binding	351 – 372	22	FAD By similarity
	Nucleotide binding	403 – 422	20	FAD By similarity
	Region	497 – 577	81	Thiamine pyrophosphate binding
Sites
	Metal binding	548	1	Magnesium By similarity
	Metal binding	575	1	Magnesium By similarity
	Binding site	134	1	Thiamine pyrophosphate By similarity
	Binding site	236	1	FAD By similarity
Experimental info
	Sequence conflict	5	1	A → V in AAA35315. Ref.1
	Sequence conflict	11	1	H → D in AAA35315. Ref.1
	Sequence conflict	289	1	A → G in AAA35315. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P36620 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: 822CEED9B8414D73	FASTA	669	73,194
	10 20 30 40 50 60 MTVLAPLRRL HTRAAFSSYG REIALQKRFL NLNSCSAVRR YGTGFSNNLR IKKLKNAFGV 70 80 90 100 110 120 VRANSTKSTS TVTTASPIKY DSSFVGKTGG EIFHDMMLKH NVKHVFGYPG GAILPVFDAI 130 140 150 160 170 180 YRSPHFEFIL PRHEQAAGHA AQAYSRVTKK PGVVLVTSGP GATNVITPIA DALADGTPLV 190 200 210 220 230 240 VFSGQVATSA IGSDAFQEAD MVGISRSCTK WNVMVKDVAD LPRRIDEAFE IATSGRPGPV 250 260 270 280 290 300 LVDLPKDVTA SVLKEPIPIL SSVPSMNRRM KEVLEEGSKN VTAKIDRVAN LLKLAKKPVI 310 320 330 340 350 360 FCGHGVLANP ECPTLLRKFS ERLQIPVTTS LLGLGAVDER SDLSLHMLGM HGSGYANMAM 370 380 390 400 410 420 QEADLILALG VRFDDRVTGN VSLFAPQARL AAAEERGGII HFDISPKNIG KVVQPTEAIE 430 440 450 460 470 480 GDVYESLKLL DSATKNIKIP SRFDWLSQIQ TWKERFPFTF TRSAPGELVK PQEVIQELDK 490 500 510 520 530 540 QTSDIKDKVT ITTGVGAHQM WAATFYRWTK PSSLVTSGGL GTMGFGLPAA IGASVAAPKD 550 560 570 580 590 600 IVIDIDGDAS FSMTGMELAT VRQFDIPVKI LILNNEEQGM VTQWQNLFYE KRYSHTHQKN 610 620 630 640 650 660 PNFVKLADAM GIKALRVEKR EDLAKKMKEF LSTKGPVLME VLVAQKEHVY PFVPGGKALH QFILHESLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and structure of an acetolactate synthase gene from Schizosaccharomyces pombe and complementation of the ilv2 mutation in Saccharomyces cerevisiae." Bekkaoui F., Nadin-Davis S.A., Crosby W.L. Curr. Genet. 24:544-547(1993) [PubMed: 8299177] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11293 Genomic DNA. Translation: AAA35315.1. CU329671 Genomic DNA. Translation: CAB87369.1.
PIR	S39111.
RefSeq	NP_595382.1. NM_001021289.1.
3D structure databases
ProteinModelPortal	P36620.
SMR	P36620. Positions 81-663.
ModBase	Search...
Protein-protein interaction databases
STRING	P36620.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBP35G2.07.1; SPBP35G2.07.1:pep; SPBP35G2.07.
GeneID	2541345.
GenomeReviews	Gene locus ilv1 in contig CU329671_GR.
KEGG	spo:SPBP35G2.07.
NMPDR	fig|4896.1.peg.1248.
Organism-specific databases
GeneDB_Spombe	SPBP35G2.07.
Phylogenomic databases
eggNOG	fuNOG05020.
GeneTree	EFGT00050000001792.
HOGENOM	HBG323037.
OMA	WVIEECA.
OrthoDB	EOG44TSH5.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003456-MONOMER.
Gene expression databases
ArrayExpress	P36620.
Family and domain databases
InterPro	IPR012846. Acetolactate_synth_lsu. IPR012000. Thiamin_PyroP_enz_cen_dom. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR000399. TPP-bd_CS. IPR011766. TPP_enzyme-bd_C. [Graphical view]
KO	K01652.
PANTHER	PTHR18968:SF13. PTHR18968:SF13. 1 hit.
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_SCHPO

Accession

Primary (citable) accession number: P36620
Secondary accession number(s): Q9P796

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 21, 2001
Last modified:	December 14, 2011
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program