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Q9P4R4

- LYS9_MAGO7

UniProt

Q9P4R4 - LYS9_MAGO7

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Protein

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

Gene
LYS3, MGG_08564
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

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
Complete GO annotation...

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.

Miscellaneous databases

EvolutionaryTraceiQ9P4R4.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: November 13, 2013
This is version 95 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

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

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