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Protein

Acetolactate synthase 1, 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 sitei129 – 1291Thiamine pyrophosphateBy similarity
Binding sitei231 – 2311FADBy similarity
Metal bindingi523 – 5231MagnesiumBy similarity
Metal bindingi550 – 5501MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi337 – 35822FADBy similarityAdd
BLAST
Nucleotide bindingi380 – 39920FADBy 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 1, chloroplastic (EC:2.2.1.6)
Alternative name(s):
ALS I
Acetohydroxy-acid synthase I
Acetolactate synthase I
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 – 8282ChloroplastBy similarityAdd
BLAST
Chaini83 – 655573Acetolactate synthase 1, chloroplasticPRO_0000035656Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP27818.
SMRiP27818. Positions 71-652.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni472 – 55281Thiamine 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.

P27818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKDSS RLHRPLAISA
60 70 80 90 100
VLNSPVNVAP PSPEKTDKNK TFVSRYAPDE PRKGADILVE ALERQGVETV
110 120 130 140 150
FAYPGGASME IHQALTRSST IRNVLPRHEQ GGVFAAEGYA RSSGKPGICI
160 170 180 190 200
ATSGPGATNL VSGLADAMLD SVPLVAITGQ VPRRMIGTDA FQETPIVEVT
210 220 230 240 250
RSITKHNYLV MDVDDIPRIV QEAFFLATSG RPGPVLVDVP KDIQQQLAIP
260 270 280 290 300
NWDQPMRLPG YMSRLPQPPE VSQLGQIVRL ISESKRPVLY VGGGSLNSSE
310 320 330 340 350
ELGRFVELTG IPVASTLMGL GSYPCNDELS LQMLGMHGTV YANYAVEHSD
360 370 380 390 400
LLLAFGVRFD DRVTGKLEAF ASRAKIVHID IDSAEIGKNK TPHVSVCGDV
410 420 430 440 450
KLALQGMNKV LENRAEELKL DFGVWRSELS EQKQKFPLSF KTFGEAIPPQ
460 470 480 490 500
YAIQILDELT EGKAIISTGV GQHQMWAAQF YKYRKPRQWL SSSGLGAMGF
510 520 530 540 550
GLPAAIGASV ANPDAIVVDI DGDGSFIMNV QELATIRVEN LPVKILLLNN
560 570 580 590 600
QHLGMVMQWE DRFYKANRAH TYLGDPAREN EIFPNMLQFA GACGIPAARV
610 620 630 640 650
TKKEELREAI QTMLDTPGPY LLDVICPHQE HVLPMIPSGG TFKDVITEGD

GRTKY
Length:655
Mass (Da):71,289
Last modified:August 1, 1992 - v1
Checksum:i1BEAD7D7A0DAD91A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11524 Genomic DNA. Translation: CAA77613.1.
PIRiS17691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11524 Genomic DNA. Translation: CAA77613.1.
PIRiS17691.

3D structure databases

ProteinModelPortaliP27818.
SMRiP27818. Positions 71-652.
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.

Entry informationi

Entry nameiILVB1_BRANA
AccessioniPrimary (citable) accession number: P27818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 7, 2015
This is version 98 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.