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Protein

Acetolactate synthase

Gene

ALS2

Organism
Brassica napus (Rape)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Note: Binds 1 magnesium ion per subunit.
  • Note: Binds 1 thiamine pyrophosphate per subunit.
  • Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation
  • thiamine diphosphateUniRule annotationNote: Binds 1 thiamine pyrophosphate per subunit.UniRule annotation

Pathway: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (BnaA05g03070D), Acetolactate synthase (ALS1), Acetolactate synthase 1, chloroplastic, Acetolactate synthase 3, chloroplastic, Acetolactate synthase (ALS2), Acetolactate synthase (ALS3), Acetolactate synthase (ALS1), Acetolactate synthase 2, chloroplastic
  2. Ketol-acid reductoisomerase (BnaC06g16700D), Ketol-acid reductoisomerase (BnaC08g29320D), Ketol-acid reductoisomerase (BnaC04g23500D), Ketol-acid reductoisomerase (BnaA04g01910D)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
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.

Pathway: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase (BnaA05g03070D), Acetolactate synthase (ALS1), Acetolactate synthase 1, chloroplastic, Acetolactate synthase 3, chloroplastic, Acetolactate synthase (ALS2), Acetolactate synthase (ALS3), Acetolactate synthase (ALS1), Acetolactate synthase 2, chloroplastic
  2. Ketol-acid reductoisomerase (BnaC06g16700D), Ketol-acid reductoisomerase (BnaC08g29320D), Ketol-acid reductoisomerase (BnaC04g23500D), Ketol-acid reductoisomerase (BnaA04g01910D)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Thiamine pyrophosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthaseUniRule annotation (EC:2.2.1.6UniRule annotation)
Gene namesi
Name:ALS2Imported
OrganismiBrassica napus (Rape)Imported
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Structurei

3D structure databases

ProteinModelPortaliQ05767.
SMRiQ05767. Positions 22-596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TPP enzyme family.UniRule annotation

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. 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.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHLLPLKKP TRTRLSSPAT LPDEPRKGAD ILVEALERQG VETVFAYPGG
60 70 80 90 100
ASMEIHQALT RSSTIRNVLP RHEQGGVFAA EGYARSSGKP GICIATSGPG
110 120 130 140 150
ATNLVSGLAD AMLDSVPLVA ITGQVPRRMI GTDAFQETPI VEVTRSITKH
160 170 180 190 200
NYLVMDVDDI PRIVQEAFFL ATSGRPGPVL VDVPKDIQQQ LAIPNWDQPM
210 220 230 240 250
RLPGYMSRLP QPPEVSQLGQ IVRLISESKR PVLYVGGGSL NSSEELGRFV
260 270 280 290 300
ELTGIPVAST LMGLGSYPCN DELSLQMLGM HGTVYANYAV EHSDLLLAFG
310 320 330 340 350
VRFDDRVTGK LEAFASRAKI VHIDIDSAEI GKNKTPHVSV CGDVKLALQG
360 370 380 390 400
MNKVLENRAE ELKLDFGVWR SELSEQKQKF PLSFKTFGEA IPPQYAIQIL
410 420 430 440 450
DELTEGKAII STGVGQHQMW AAQFYKYRKP RQWLSSSGLG AMGFGLPAAI
460 470 480 490 500
GASVANPDAI VVDIDGDGSF IMNVQELATI RVENLPVKIL LLNNQHLGMV
510 520 530 540 550
MQWEDRFYKA NRAHTYLGDP ARENEIFPNM LQFAGACGIP AARVTKKEEL
560 570 580 590
REAIQTMLDT PGPYLLDVIC PHQEHVLPMI PSGGTFKDVI TEGDGRTKY
Length:599
Mass (Da):65,458
Last modified:November 1, 1996 - v1
Checksum:i00CD148858DFD91A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60068 mRNA. Translation: AAA62705.1.
PIRiS15004.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60068 mRNA. Translation: AAA62705.1.
PIRiS15004.

3D structure databases

ProteinModelPortaliQ05767.
SMRiQ05767. Positions 22-596.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. 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.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Isolation, structure and expression of a cDNA for acetolactate synthase from Brassica napus."
    Bekkaoui F., Condie J.A., Neustaedter D.A., Moloney M.M., Crosby W.L.
    Plant Mol. Biol. 16:741-744(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: WestarImported.

Entry informationi

Entry nameiQ05767_BRANA
AccessioniPrimary (citable) accession number: Q05767
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: February 4, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.