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P27819

- ILVB3_BRANA

UniProt

P27819 - ILVB3_BRANA

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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 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

  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-KW
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:
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: October 29, 2014
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