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Protein

Acetolactate synthase 2, chloroplastic

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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

Pathway:iL-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 (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 (BnaC08g29320D), Ketol-acid reductoisomerase (BnaC06g16700D), 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:iL-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 (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 (BnaC08g29320D), Ketol-acid reductoisomerase (BnaC06g16700D), 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Thiamine pyrophosphateBy similarity
Binding sitei222 – 2221FADBy similarity
Metal bindingi513 – 5131MagnesiumBy similarity
Metal bindingi540 – 5401MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi329 – 35022FADBy similarityAdd
BLAST
Nucleotide bindingi372 – 39120FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Herbicide resistance

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase 2, chloroplastic (EC:2.2.1.6)
Alternative name(s):
ALS II
Acetohydroxy-acid synthase II
Acetolactate synthase II
OrganismiBrassica napus (Rape)
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7373ChloroplastBy similarityAdd
BLAST
Chaini74 – 637564Acetolactate synthase 2, chloroplasticPRO_0000035657Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP14874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni462 – 54281Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Keywords - Domaini

Transit peptide

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFSFFGTI PSSPTKASVF SLPVSVTTLP SFPRRRATRV SVSANSKKDQ
60 70 80 90 100
DRTASRRENP STFSSKYAPN VPRSGADILV EALERQGVDV VFAYPGGASM
110 120 130 140 150
EIHQALTRSN TIRNVLPRHE QGGIFAAEGY ARSSGKPGIC IATSGPGAMN
160 170 180 190 200
LVSGLADALF DSVPLIAITG QVPRRMIGTM AFQETPVVEV TRTITKHNYL
210 220 230 240 250
VMEVDDIPRI VREAFFLATS VRPGPVLIDV PKDVQQQFAI PNWEQPMRLP
260 270 280 290 300
LYMSTMPKPP KVSHLEQILR LVSESKRPVL YVGGGCLNSS EELRRFVELT
310 320 330 340 350
GIPVASTFMG LGSYPCDDEE FSLQMLGMHG TVYANYAVEY SDLLLAFGVR
360 370 380 390 400
FDDRVTGKLE AFASRAKIVH IDIDSTEIGK NKTPHVSVCC DVQLALQGMN
410 420 430 440 450
EVLENRRDVL DFGEWRCELN EQRLKFPLRY KTFGEEIPPQ YAIQLLDELT
460 470 480 490 500
DGKAIITTGV GQHQMWAAQF YRFKKPRQWL SSGGLGAMGF GLPAAMGAAI
510 520 530 540 550
ANPGAVVVDI DGDGSFIMNI QELATIRVEN LPVKVLLINN QHLGMVLQWE
560 570 580 590 600
DHFYAANRAD SFLGDPANPE AVFPDMLLFA ASCGIPAARV TRREDLREAI
610 620 630
QTMLDTPGPF LLDVVCPHQD HVLPLIPSGG TFKDIIV
Length:637
Mass (Da):69,970
Last modified:April 1, 1990 - v1
Checksum:i9FC6A6E8124C2455
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11525 Genomic DNA. Translation: CAA77614.1.
X16708 Genomic DNA. Translation: CAA34680.1.
PIRiJQ0357. YCRP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11525 Genomic DNA. Translation: CAA77614.1.
X16708 Genomic DNA. Translation: CAA34680.1.
PIRiJQ0357. YCRP.

3D structure databases

ProteinModelPortaliP14874.
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. "Molecular characterization and genetic origin of the Brassica napus acetohydroxyacid synthase multigene family."
    Rutledge R.G., Ouellet T., Hattori J., Miki B.L.A.
    Mol. Gen. Genet. 229:31-40(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Topas.
  2. "Isolation, expression and phylogenetic inheritance of an acetolactate synthase gene from Brassica napus."
    Wiersma P.A., Schmiemann M.G., Condie J.A., Crosby W.L., Moloney M.M.
    Mol. Gen. Genet. 219:413-420(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Westar.
    Tissue: Leaf.

Entry informationi

Entry nameiILVB2_BRANA
AccessioniPrimary (citable) accession number: P14874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Acetolactate synthase is the target enzyme for sulfonylurea and imidazolinone herbicides.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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.