Reviewed, UniProtKB/Swiss-Prot P45261 (ILVI_HAEIN)

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:	HI1585

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	573 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 – 573	573	Acetolactate synthase large subunit		PRO_0000090795
Regions
	Nucleotide binding	261 – 282	22	FAD By similarity
	Nucleotide binding	304 – 323	20	FAD By similarity
	Region	396 – 476	81	Thiamine pyrophosphate binding
Sites
	Metal binding	447	1	Magnesium By similarity
	Metal binding	474	1	Magnesium By similarity
	Binding site	51	1	Thiamine pyrophosphate By similarity
	Binding site	153	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45261-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: CA055388605F60BE	FASTA	573	62,620
	10 20 30 40 50 60 MKKLSGAEMV VQSLRDEGVE YVFGYPGGAV LDIYDAIHTL GGIEHILVRH EQAAVHMADG 70 80 90 100 110 120 YARSTGKVGC VLVTSGPGAT NAITGILTAY TDSVPMVIIS GQVMSNLIGS DAFQECDMLG 130 140 150 160 170 180 ISRPVVKHSF IVKKAEDIPS TLKKAFYIAS TGRPGPVVVD IPKDTVNPNF KYPYEYPEYV 190 200 210 220 230 240 ELRSYNPTVN GHKGQIKKAL KALLVAKKPI LFVGGGAITA ECSEQLIQFA QRLNLPVTSS 250 260 270 280 290 300 LMGLGAYPST DKQFLGMLGM HGTLEANTAM HESDLILGIG VRFDDRTTNN LEKYCPNAKV 310 320 330 340 350 360 IHIDIDPTSI SKNVPVAIPI VGNAKNVLEE FLGLLNEEGL KSQTDLESWW QEINQWKAKK 370 380 390 400 410 420 CLEFDRTSGV IKPQQVVEAV YRLTKGQAYV ASDVGQHQMF AALHYPFDEP RHWINSGGAG 430 440 450 460 470 480 TMGFGFPAAL GVKLAHPEGT VVCVTGDGSI QMNIQELSTA TQYGIPVVII CLNNHFLGMV 490 500 510 520 530 540 KQWQDLIYSG RHSQTYMNSL PDFAKLAESY GHVGIKIATP DELESKLQEA FSIKNKLVFV 550 560 570 DINVDESEHV YPMQIRGGAM NEMILSKPQE ETN

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC23233.1.
PIR	C64131.
RefSeq	NP_439730.1.
3D structure databases
HSSP	HSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	950449.
GenomeReviews	Gene locus HI1585 in contig L42023_GR.
KEGG	hin:HI1585.
NMPDR	fig|71421.1.peg.1505.
TIGR	HI1585.
Phylogenomic databases
HOGENOM	P45261.
OMA	P45261. QFRLPVK.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1585-MON.
BRENDA	2.2.1.6. 109.
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_HAEIN

Accession

Primary (citable) accession number: P45261

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 68 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)