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Q9P4R4 (LYS9_MAGO7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]

EC=1.5.1.10
Alternative name(s):
Saccharopine reductase
Gene names
Name:LYS3
ORF Names:MGG_08564
OrganismMagnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Pyricularia oryzae) [Complete proteome]
Taxonomic identifier242507 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeMagnaporthalesMagnaporthaceaeMagnaporthe

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 2/3.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the saccharopine dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Lysine biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processlysine biosynthetic process via aminoadipic acid

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionsaccharopine dehydrogenase (NADP+, L-glutamate-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]
PRO_0000212838

Natural variations

Natural variant1401E → G in strain: 4091-5-8.
Natural variant3981L → F in strain: 4091-5-8.

Secondary structure

................................................................................. 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9P4R4 [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: 9997B94CF1245035

FASTA45049,097
        10         20         30         40         50         60 
MATKSVLMLG SGFVTRPTLD VLTDSGIKVT VACRTLESAK KLSAGVQHST PISLDVNDDA 

        70         80         90        100        110        120 
ALDAEVAKHD LVISLIPYTF HATVIKSAIR QKKHVVTTSY VSPAMMELDQ AAKDAGITVM 

       130        140        150        160        170        180 
NEIGLDPGID HLYAIKTIEE VHAAGGKIKT FLSYCGGLPA PESSDNPLGY KFSWSSRGVL 

       190        200        210        220        230        240 
LALRNAASFY KDGKVTNVAG PELMATAKPY FIYPGFAFVA YPNRDSTPYK ERYQIPEADN 

       250        260        270        280        290        300 
IVRGTLRYQG FPQFIKVLVD IGFLSDEEQP FLKEAIPWKE ATQKIVKASS ASEQDIVSTI 

       310        320        330        340        350        360 
VSNATFESTE EQKRIVAGLK WLGIFSDKKI TPRGNALDTL CATLEEKMQF EEGERDLVML 

       370        380        390        400        410        420 
QHKFEIENKD GSRETRTSSL CEYGAPIGSG GYSAMAKLVG VPCAVAVKFV LDGTISDRGV 

       430        440        450 
LAPMNSKIND PLMKELKEKY GIECKEKVVA 

« Hide

References

« Hide 'large scale' references
[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]"The genome sequence of the rice blast fungus Magnaporthe grisea."
Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M. expand/collapse author list , Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.
Nature 434:980-986(2005) [PubMed] [Europe PMC] [Abstract]
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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF144424 Genomic DNA. Translation: AAF91081.1.
CM001234 Genomic DNA. Translation: EHA49766.1.
RefSeqXP_003716085.1. XM_003716037.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5LX-ray2.40A/B1-450[»]
1E5QX-ray2.10A/B/C/D/E/F/G/H1-450[»]
1FF9X-ray2.00A1-450[»]
ProteinModelPortalQ9P4R4.
SMRQ9P4R4. Positions 2-450.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiMGG_17041T0; MGG_17041T0; MGG_17041.
GeneID12984319.
KEGGmgr:MGG_17041.

Phylogenomic databases

eggNOGCOG1748.
KOK00293.
OrthoDBEOG7FJH8S.

Enzyme and pathway databases

UniPathwayUPA00033; UER00033.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR016040. NAD(P)-bd_dom.
IPR005097. Saccharopine_DH/HSpermid_syn.
[Graphical view]
PfamPF03435. Saccharop_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9P4R4.

Entry information

Entry nameLYS9_MAGO7
AccessionPrimary (citable) accession number: Q9P4R4
Secondary accession number(s): A4QYG4, G4N642
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: June 12, 2007
Last modified: November 13, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways