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P27819

- ILVB3_BRANA

UniProt

P27819 - ILVB3_BRANA

Protein

Acetolactate synthase 3, chloroplastic

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    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

    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

    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

    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: October 1, 2014
    This is version 97 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