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Q05767

- Q05767_BRANA

UniProt

Q05767 - Q05767_BRANA

Protein

Acetolactate synthase

Gene

ALS2

Organism
Brassica napus (Rape)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    2 pyruvate = 2-acetolactate + CO2.

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation
    Binds 1 thiamine pyrophosphate per subunit.UniRule annotation

    Pathwayi

    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. valine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    TransferaseUniRule annotation

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Thiamine pyrophosphateUniRule annotation

    Enzyme and pathway databases

    UniPathwayiUPA00047; UER00055.
    UPA00049; UER00059.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetolactate synthaseUniRule annotation (EC:2.2.1.6UniRule annotation)
    Gene namesi
    Name:ALS2Imported
    OrganismiBrassica napus (Rape)Imported
    Taxonomic identifieri3708 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

    Structurei

    3D structure databases

    ProteinModelPortaliQ05767.
    SMRiQ05767. Positions 22-596.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TPP enzyme family.UniRule annotation

    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.

    Q05767-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHLLPLKKP TRTRLSSPAT LPDEPRKGAD ILVEALERQG VETVFAYPGG    50
    ASMEIHQALT RSSTIRNVLP RHEQGGVFAA EGYARSSGKP GICIATSGPG 100
    ATNLVSGLAD AMLDSVPLVA ITGQVPRRMI GTDAFQETPI VEVTRSITKH 150
    NYLVMDVDDI PRIVQEAFFL ATSGRPGPVL VDVPKDIQQQ LAIPNWDQPM 200
    RLPGYMSRLP QPPEVSQLGQ IVRLISESKR PVLYVGGGSL NSSEELGRFV 250
    ELTGIPVAST LMGLGSYPCN DELSLQMLGM HGTVYANYAV EHSDLLLAFG 300
    VRFDDRVTGK LEAFASRAKI VHIDIDSAEI GKNKTPHVSV CGDVKLALQG 350
    MNKVLENRAE ELKLDFGVWR SELSEQKQKF PLSFKTFGEA IPPQYAIQIL 400
    DELTEGKAII STGVGQHQMW AAQFYKYRKP RQWLSSSGLG AMGFGLPAAI 450
    GASVANPDAI VVDIDGDGSF IMNVQELATI RVENLPVKIL LLNNQHLGMV 500
    MQWEDRFYKA NRAHTYLGDP ARENEIFPNM LQFAGACGIP AARVTKKEEL 550
    REAIQTMLDT PGPYLLDVIC PHQEHVLPMI PSGGTFKDVI TEGDGRTKY 599
    Length:599
    Mass (Da):65,458
    Last modified:November 1, 1996 - v1
    Checksum:i00CD148858DFD91A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60068 mRNA. Translation: AAA62705.1.
    PIRiS15004.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60068 mRNA. Translation: AAA62705.1 .
    PIRi S15004.

    3D structure databases

    ProteinModelPortali Q05767.
    SMRi Q05767. Positions 22-596.
    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. "Isolation, structure and expression of a cDNA for acetolactate synthase from Brassica napus."
      Bekkaoui F., Condie J.A., Neustaedter D.A., Moloney M.M., Crosby W.L.
      Plant Mol. Biol. 16:741-744(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: WestarImported.

    Entry informationi

    Entry nameiQ05767_BRANA
    AccessioniPrimary (citable) accession number: Q05767
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 1, 1996
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)