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.

P27819

- ILVB3_BRANA

UniProt

P27819 - ILVB3_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 3, 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 sitei126 – 1261Thiamine pyrophosphate By similarity
Binding sitei228 – 2281FAD By similarity
Metal bindingi520 – 5201Magnesium By similarity
Metal bindingi547 – 5471Magnesium By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi334 – 35522FAD By similarity
Add
BLAST
Nucleotide bindingi377 – 39620FAD By similarity
Add
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 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

  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 – 6969Chloroplast By similarity
Add
BLAST
Chaini70 – 652583Acetolactate synthase 3, chloroplastic
PRO_0000035658Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP27819.
SMRiP27819. Positions 68-649.

Family & Domainsi

Region

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

P27819-1 [UniParc]FASTAAdd to Basket

« Hide

MAAATSSSPI SLTAKPSSKS PLPISRFSLP FSLTPQKPSS RLHRPLAISA    50
VLNSPVNVAP EKTDKIKTFI SRYAPDEPRK GADILVEALE RQGVETVFAY 100
PGGASMEIHQ ALTRSSTIRN VLPRHEQGGV FAAEGYARSS GKPGICIATS 150
GPGATNLVSG LADAMLDSVP LVAITGQVPR RMIGTDAFQE TPIVEVTRSI 200
TKHNYLVMDV DDIPRIVQEA FFLATSGRPG PVLVDVPKDI QQQLAIPNWD 250
QPMRLPGYMS RLPQPPEVSQ LGQIVRLISE SKRPVLYVGG GSLNSSEELG 300
RFVELTGIPV ASTLMGLGSY PCNDELSLQM LGMHGTVYAN YAVEHSDLLL 350
AFGVRFDDRV TGKLEAFASR AKIVHIDIDS AEIGKNKTPH VSVCGDVKLA 400
LQGMNKVLEN RAEELKLDFG VWRSELSEQK QKFPLSFKTF GEAIPPQYAI 450
QVLDELTQGK AIISTGVGQH QMWAAQFYKY RKPRQWLSSS GLGAMGFGLP 500
AAIGASVANP DAIVVDIDGD GSFIMNVQEL ATIRVENLPV KILLLNNQHL 550
GMVMQWEDRF YKANRAHTYL GDPARENEIF PNMLQFAGAC GIPAARVTKK 600
EELREAIQTM LDTPGPYLLD VICPHQEHVL PMIPSGGTFK DVITEGDGRT 650
KY 652
Length:652
Mass (Da):70,988
Last modified:August 1, 1992 - v1
Checksum:iB12534C50CC5AE0D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11526 Genomic DNA. Translation: CAA77615.1.
PIRiS29838.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11526 Genomic DNA. Translation: CAA77615.1 .
PIRi S29838.

3D structure databases

ProteinModelPortali P27819.
SMRi P27819. Positions 68-649.
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.
  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: June 11, 2014
This is version 96 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