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Protein

Acetolactate synthase 3, 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: 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 (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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Thiamine pyrophosphateBy similarity
Binding sitei228 – 2281FADBy similarity
Metal bindingi520 – 5201MagnesiumBy similarity
Metal bindingi547 – 5471MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi334 – 35522FADBy similarityAdd
BLAST
Nucleotide bindingi377 – 39620FADBy 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 3, chloroplastic (EC:2.2.1.6)
Alternative name(s):
ALS III
Acetohydroxy-acid synthase III
Acetolactate synthase III
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 – 6969ChloroplastBy similarityAdd
BLAST
Chaini70 – 652583Acetolactate synthase 3, chloroplasticPRO_0000035658Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP27819.
SMRiP27819. Positions 68-649.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni469 – 54981Thiamine 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.

P27819-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKPSS RLHRPLAISA
60 70 80 90 100
VLNSPVNVAP EKTDKIKTFI SRYAPDEPRK GADILVEALE RQGVETVFAY
110 120 130 140 150
PGGASMEIHQ ALTRSSTIRN VLPRHEQGGV FAAEGYARSS GKPGICIATS
160 170 180 190 200
GPGATNLVSG LADAMLDSVP LVAITGQVPR RMIGTDAFQE TPIVEVTRSI
210 220 230 240 250
TKHNYLVMDV DDIPRIVQEA FFLATSGRPG PVLVDVPKDI QQQLAIPNWD
260 270 280 290 300
QPMRLPGYMS RLPQPPEVSQ LGQIVRLISE SKRPVLYVGG GSLNSSEELG
310 320 330 340 350
RFVELTGIPV ASTLMGLGSY PCNDELSLQM LGMHGTVYAN YAVEHSDLLL
360 370 380 390 400
AFGVRFDDRV TGKLEAFASR AKIVHIDIDS AEIGKNKTPH VSVCGDVKLA
410 420 430 440 450
LQGMNKVLEN RAEELKLDFG VWRSELSEQK QKFPLSFKTF GEAIPPQYAI
460 470 480 490 500
QVLDELTQGK AIISTGVGQH QMWAAQFYKY RKPRQWLSSS GLGAMGFGLP
510 520 530 540 550
AAIGASVANP DAIVVDIDGD GSFIMNVQEL ATIRVENLPV KILLLNNQHL
560 570 580 590 600
GMVMQWEDRF YKANRAHTYL GDPARENEIF PNMLQFAGAC GIPAARVTKK
610 620 630 640 650
EELREAIQTM LDTPGPYLLD VICPHQEHVL PMIPSGGTFK DVITEGDGRT

KY
Length:652
Mass (Da):70,988
Last modified:August 1, 1992 - v1
Checksum:iB12534C50CC5AE0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11526 Genomic DNA. Translation: CAA77615.1.
PIRiS29838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11526 Genomic DNA. Translation: CAA77615.1.
PIRiS29838.

3D structure databases

ProteinModelPortaliP27819.
SMRiP27819. Positions 68-649.
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. Miki B.L.
    Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiILVB3_BRANA
AccessioniPrimary (citable) accession number: P27819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 7, 2015
This is version 100 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.