SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P27818

- ILVB1_BRANA

UniProt

P27818 - ILVB1_BRANA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Acetolactate synthase 1, chloroplastic

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

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Binds 1 magnesium ion per subunit By similarity.
Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291Thiamine pyrophosphate By similarity
Binding sitei231 – 2311FAD By similarity
Metal bindingi523 – 5231Magnesium By similarity
Metal bindingi550 – 5501Magnesium By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi337 – 35822FAD By similarityAdd
BLAST
Nucleotide bindingi380 – 39920FAD By similarityAdd
BLAST

GO - Molecular functioni

  1. acetolactate synthase activity Source: UniProtKB-EC
  2. flavin adenine dinucleotide binding Source: InterPro
  3. magnesium ion binding Source: InterPro
  4. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. isoleucine biosynthetic process Source: UniProtKB-UniPathway
  2. response to herbicide Source: UniProtKB-KW
  3. valine biosynthetic process Source: UniProtKB-UniPathway
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

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8282Chloroplast By similarityAdd
BLAST
Chaini83 – 655573Acetolactate synthase 1, chloroplasticPRO_0000035656Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP27818.
SMRiP27818. Positions 71-652.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni472 – 55281Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.

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

MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKDSS RLHRPLAISA    50
VLNSPVNVAP PSPEKTDKNK TFVSRYAPDE PRKGADILVE ALERQGVETV 100
FAYPGGASME IHQALTRSST IRNVLPRHEQ GGVFAAEGYA RSSGKPGICI 150
ATSGPGATNL VSGLADAMLD SVPLVAITGQ VPRRMIGTDA FQETPIVEVT 200
RSITKHNYLV MDVDDIPRIV QEAFFLATSG RPGPVLVDVP KDIQQQLAIP 250
NWDQPMRLPG YMSRLPQPPE VSQLGQIVRL ISESKRPVLY VGGGSLNSSE 300
ELGRFVELTG IPVASTLMGL GSYPCNDELS LQMLGMHGTV YANYAVEHSD 350
LLLAFGVRFD DRVTGKLEAF ASRAKIVHID IDSAEIGKNK TPHVSVCGDV 400
KLALQGMNKV LENRAEELKL DFGVWRSELS EQKQKFPLSF KTFGEAIPPQ 450
YAIQILDELT EGKAIISTGV GQHQMWAAQF YKYRKPRQWL SSSGLGAMGF 500
GLPAAIGASV ANPDAIVVDI DGDGSFIMNV QELATIRVEN LPVKILLLNN 550
QHLGMVMQWE DRFYKANRAH TYLGDPAREN EIFPNMLQFA GACGIPAARV 600
TKKEELREAI QTMLDTPGPY LLDVICPHQE HVLPMIPSGG TFKDVITEGD 650
GRTKY 655
Length:655
Mass (Da):71,289
Last modified:August 1, 1992 - v1
Checksum:i1BEAD7D7A0DAD91A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11524 Genomic DNA. Translation: CAA77613.1.
PIRiS17691.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11524 Genomic DNA. Translation: CAA77613.1 .
PIRi S17691.

3D structure databases

ProteinModelPortali P27818.
SMRi P27818. Positions 71-652.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00047 ; UER00055 .
UPA00049 ; UER00059 .

Family and domain databases

Gene3Di 3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProi 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.
[Graphical view ]
Pfami PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view ]
SUPFAMi SSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00118. acolac_lg. 1 hit.
PROSITEi PS00187. TPP_ENZYMES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 94 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