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Protein

Acetolactate synthase large subunit

Gene

ilvI

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit (ilvH), Acetolactate synthase large subunit (ilvI)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit (ilvH), Acetolactate synthase large subunit (ilvI)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei51Thiamine pyrophosphateBy similarity1
Binding sitei153FADBy similarity1
Metal bindingi447MagnesiumBy similarity1
Metal bindingi474MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi261 – 282FADBy similarityAdd BLAST22
Nucleotide bindingi304 – 323FADBy similarityAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandFAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciHINF71421:G1GJ1-1601-MONOMER.
BRENDAi2.2.1.6. 2529.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase large subunit (EC:2.2.1.6)
Short name:
AHAS
Alternative name(s):
Acetohydroxy-acid synthase large subunit
Short name:
ALS
Gene namesi
Name:ilvI
Ordered Locus Names:HI_1585
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000907951 – 573Acetolactate synthase large subunitAdd BLAST573

Interactioni

Subunit structurei

Dimer of large and small chains.By similarity

Protein-protein interaction databases

STRINGi71421.HI1585.

Structurei

3D structure databases

ProteinModelPortaliP45261.
SMRiP45261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni396 – 476Thiamine pyrophosphate bindingAdd BLAST81

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
KOiK01652.
OMAiQGMVRQW.
PhylomeDBiP45261.

Family and domain databases

InterProiView protein in InterPro
IPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
PfamiView protein in Pfam
PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiView protein in PROSITE
PS00187. TPP_ENZYMES. 1 hit.

Sequencei

Sequence statusi: Complete.

P45261-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLSGAEMV VQSLRDEGVE YVFGYPGGAV LDIYDAIHTL GGIEHILVRH
60 70 80 90 100
EQAAVHMADG YARSTGKVGC VLVTSGPGAT NAITGILTAY TDSVPMVIIS
110 120 130 140 150
GQVMSNLIGS DAFQECDMLG ISRPVVKHSF IVKKAEDIPS TLKKAFYIAS
160 170 180 190 200
TGRPGPVVVD IPKDTVNPNF KYPYEYPEYV ELRSYNPTVN GHKGQIKKAL
210 220 230 240 250
KALLVAKKPI LFVGGGAITA ECSEQLIQFA QRLNLPVTSS LMGLGAYPST
260 270 280 290 300
DKQFLGMLGM HGTLEANTAM HESDLILGIG VRFDDRTTNN LEKYCPNAKV
310 320 330 340 350
IHIDIDPTSI SKNVPVAIPI VGNAKNVLEE FLGLLNEEGL KSQTDLESWW
360 370 380 390 400
QEINQWKAKK CLEFDRTSGV IKPQQVVEAV YRLTKGQAYV ASDVGQHQMF
410 420 430 440 450
AALHYPFDEP RHWINSGGAG TMGFGFPAAL GVKLAHPEGT VVCVTGDGSI
460 470 480 490 500
QMNIQELSTA TQYGIPVVII CLNNHFLGMV KQWQDLIYSG RHSQTYMNSL
510 520 530 540 550
PDFAKLAESY GHVGIKIATP DELESKLQEA FSIKNKLVFV DINVDESEHV
560 570
YPMQIRGGAM NEMILSKPQE ETN
Length:573
Mass (Da):62,620
Last modified:November 1, 1995 - v1
Checksum:iCA055388605F60BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC23233.1.
PIRiC64131.
RefSeqiNP_439730.1. NC_000907.1.
WP_005671546.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC23233; AAC23233; HI_1585.
GeneIDi950449.
KEGGihin:HI1585.
PATRICifig|71421.8.peg.1659.

Similar proteinsi

Entry informationi

Entry nameiILVI_HAEIN
AccessioniPrimary (citable) accession number: P45261
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome