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Q9P4R4

- LYS9_MAGO7

UniProt

Q9P4R4 - LYS9_MAGO7

Protein

Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]

Gene

LYS3

Organism
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (12 Jun 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH.

    Pathwayi

    GO - Molecular functioni

    1. saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity Source: UniProtKB-EC

    GO - Biological processi

    1. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00033; UER00033.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (EC:1.5.1.10)
    Alternative name(s):
    Saccharopine reductase
    Gene namesi
    Name:LYS3
    ORF Names:MGG_08564
    OrganismiMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae)
    Taxonomic identifieri242507 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe
    ProteomesiUP000009058: Chromosome 4

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]PRO_0000212838Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    450
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi15 – 239
    Turni24 – 263
    Beta strandi28 – 358
    Helixi36 – 416
    Turni42 – 454
    Beta strandi49 – 535
    Helixi59 – 668
    Beta strandi69 – 746
    Helixi78 – 803
    Helixi81 – 9111
    Beta strandi94 – 996
    Helixi103 – 1075
    Helixi109 – 1146
    Beta strandi118 – 1203
    Turni125 – 1273
    Helixi129 – 14315
    Beta strandi147 – 15913
    Helixi161 – 1633
    Beta strandi172 – 1743
    Helixi176 – 1827
    Beta strandi187 – 1915
    Beta strandi194 – 1985
    Helixi201 – 2055
    Beta strandi218 – 2225
    Helixi229 – 2324
    Beta strandi239 – 24810
    Helixi251 – 26010
    Turni261 – 2644
    Helixi270 – 2723
    Helixi278 – 2869
    Beta strandi289 – 2924
    Helixi293 – 30311
    Helixi309 – 32214
    Turni323 – 3253
    Beta strandi326 – 3294
    Helixi336 – 34712
    Beta strandi356 – 36712
    Beta strandi373 – 38311
    Beta strandi389 – 3913
    Helixi394 – 41118
    Beta strandi419 – 4213
    Helixi426 – 44015
    Beta strandi445 – 4495

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E5LX-ray2.40A/B1-450[»]
    1E5QX-ray2.10A/B/C/D/E/F/G/H1-450[»]
    1FF9X-ray2.00A1-450[»]
    ProteinModelPortaliQ9P4R4.
    SMRiQ9P4R4. Positions 2-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P4R4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the saccharopine dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1748.
    KOiK00293.
    OrthoDBiEOG7FJH8S.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR005097. Saccharopine_DH/HSpermid_syn.
    [Graphical view]
    PfamiPF03435. Saccharop_dh. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9P4R4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATKSVLMLG SGFVTRPTLD VLTDSGIKVT VACRTLESAK KLSAGVQHST    50
    PISLDVNDDA ALDAEVAKHD LVISLIPYTF HATVIKSAIR QKKHVVTTSY 100
    VSPAMMELDQ AAKDAGITVM NEIGLDPGID HLYAIKTIEE VHAAGGKIKT 150
    FLSYCGGLPA PESSDNPLGY KFSWSSRGVL LALRNAASFY KDGKVTNVAG 200
    PELMATAKPY FIYPGFAFVA YPNRDSTPYK ERYQIPEADN IVRGTLRYQG 250
    FPQFIKVLVD IGFLSDEEQP FLKEAIPWKE ATQKIVKASS ASEQDIVSTI 300
    VSNATFESTE EQKRIVAGLK WLGIFSDKKI TPRGNALDTL CATLEEKMQF 350
    EEGERDLVML QHKFEIENKD GSRETRTSSL CEYGAPIGSG GYSAMAKLVG 400
    VPCAVAVKFV LDGTISDRGV LAPMNSKIND PLMKELKEKY GIECKEKVVA 450
    Length:450
    Mass (Da):49,097
    Last modified:June 12, 2007 - v2
    Checksum:i9997B94CF1245035
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401E → G in strain: 4091-5-8.
    Natural varianti398 – 3981L → F in strain: 4091-5-8.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144424 Genomic DNA. Translation: AAF91081.1.
    CM001234 Genomic DNA. Translation: EHA49766.1.
    RefSeqiXP_003716085.1. XM_003716037.1.

    Genome annotation databases

    EnsemblFungiiMGG_17041T0; MGG_17041T0; MGG_17041.
    GeneIDi12984319.
    KEGGimgr:MGG_17041.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144424 Genomic DNA. Translation: AAF91081.1 .
    CM001234 Genomic DNA. Translation: EHA49766.1 .
    RefSeqi XP_003716085.1. XM_003716037.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E5L X-ray 2.40 A/B 1-450 [» ]
    1E5Q X-ray 2.10 A/B/C/D/E/F/G/H 1-450 [» ]
    1FF9 X-ray 2.00 A 1-450 [» ]
    ProteinModelPortali Q9P4R4.
    SMRi Q9P4R4. Positions 2-450.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii MGG_17041T0 ; MGG_17041T0 ; MGG_17041 .
    GeneIDi 12984319.
    KEGGi mgr:MGG_17041.

    Phylogenomic databases

    eggNOGi COG1748.
    KOi K00293.
    OrthoDBi EOG7FJH8S.

    Enzyme and pathway databases

    UniPathwayi UPA00033 ; UER00033 .

    Miscellaneous databases

    EvolutionaryTracei Q9P4R4.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR016040. NAD(P)-bd_dom.
    IPR005097. Saccharopine_DH/HSpermid_syn.
    [Graphical view ]
    Pfami PF03435. Saccharop_dh. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea."
      Johansson E., Steffens J.J., Emptage M., Lindqvist Y., Schneider G.
      Acta Crystallogr. D 56:662-664(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CRYSTALLIZATION.
      Strain: 4091-5-8.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 70-15 / ATCC MYA-4617 / FGSC 8958.
    3. "Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis."
      Johansson E., Steffens J.J., Lindqvist Y., Schneider G.
      Structure 8:1037-1047(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiLYS9_MAGO7
    AccessioniPrimary (citable) accession number: Q9P4R4
    Secondary accession number(s): A4QYG4, G4N642
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2003
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3