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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: 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

BRENDAi1.5.1.10. 5238.
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 Componenti: Chromosome 4

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: EnsemblFungi
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ9P4R4.
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

        10         20         30         40         50
MATKSVLMLG SGFVTRPTLD VLTDSGIKVT VACRTLESAK KLSAGVQHST
60 70 80 90 100
PISLDVNDDA ALDAEVAKHD LVISLIPYTF HATVIKSAIR QKKHVVTTSY
110 120 130 140 150
VSPAMMELDQ AAKDAGITVM NEIGLDPGID HLYAIKTIEE VHAAGGKIKT
160 170 180 190 200
FLSYCGGLPA PESSDNPLGY KFSWSSRGVL LALRNAASFY KDGKVTNVAG
210 220 230 240 250
PELMATAKPY FIYPGFAFVA YPNRDSTPYK ERYQIPEADN IVRGTLRYQG
260 270 280 290 300
FPQFIKVLVD IGFLSDEEQP FLKEAIPWKE ATQKIVKASS ASEQDIVSTI
310 320 330 340 350
VSNATFESTE EQKRIVAGLK WLGIFSDKKI TPRGNALDTL CATLEEKMQF
360 370 380 390 400
EEGERDLVML QHKFEIENKD GSRETRTSSL CEYGAPIGSG GYSAMAKLVG
410 420 430 440 450
VPCAVAVKFV LDGTISDRGV LAPMNSKIND PLMKELKEKY GIECKEKVVA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF144424 Genomic DNA. Translation: AAF91081.1.
CM001234 Genomic DNA. Translation: EHA49766.1.
RefSeqiXP_003716085.1. XM_003716037.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG1748.
InParanoidiQ9P4R4.
KOiK00293.
OrthoDBiEOG7FJH8S.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00033.
BRENDAi1.5.1.10. 5238.

Miscellaneous databases

EvolutionaryTraceiQ9P4R4.

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]
ProtoNetiSearch...

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(1999) [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(1999) [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: April 1, 2015
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.