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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: L-lysine biosynthesis via AAA pathway

This protein is involved in step 2 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. L-aminoadipate-semialdehyde dehydrogenase (MGCH7_ch7g332)
  2. Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (LYS3)
  3. Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (MGG_01359)
This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route), the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000009058 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiFungiDB:MGG_17041.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002128381 – 450Saccharopine dehydrogenase [NADP(+), L-glutamate-forming]Add BLAST450

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi15 – 23Combined sources9
Turni24 – 26Combined sources3
Beta strandi28 – 35Combined sources8
Helixi36 – 41Combined sources6
Turni42 – 45Combined sources4
Beta strandi49 – 53Combined sources5
Helixi59 – 66Combined sources8
Beta strandi69 – 74Combined sources6
Helixi78 – 80Combined sources3
Helixi81 – 91Combined sources11
Beta strandi94 – 99Combined sources6
Helixi103 – 107Combined sources5
Helixi109 – 114Combined sources6
Beta strandi118 – 120Combined sources3
Turni125 – 127Combined sources3
Helixi129 – 143Combined sources15
Beta strandi147 – 159Combined sources13
Helixi161 – 163Combined sources3
Beta strandi172 – 174Combined sources3
Helixi176 – 182Combined sources7
Beta strandi187 – 191Combined sources5
Beta strandi194 – 198Combined sources5
Helixi201 – 205Combined sources5
Beta strandi218 – 222Combined sources5
Helixi229 – 232Combined sources4
Beta strandi239 – 248Combined sources10
Helixi251 – 260Combined sources10
Turni261 – 264Combined sources4
Helixi270 – 272Combined sources3
Helixi278 – 286Combined sources9
Beta strandi289 – 292Combined sources4
Helixi293 – 303Combined sources11
Helixi309 – 322Combined sources14
Turni323 – 325Combined sources3
Beta strandi326 – 329Combined sources4
Helixi336 – 347Combined sources12
Beta strandi356 – 367Combined sources12
Beta strandi373 – 383Combined sources11
Beta strandi389 – 391Combined sources3
Helixi394 – 411Combined sources18
Beta strandi419 – 421Combined sources3
Helixi426 – 440Combined sources15
Beta strandi445 – 449Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P4R4.

Family & Domainsi

Sequence similaritiesi

Belongs to the saccharopine dehydrogenase family.Curated

Phylogenomic databases

InParanoidiQ9P4R4.
KOiK00293.
OrthoDBiEOG092C2J3O.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR032095. Sacchrp_dh_C.
IPR005097. Sacchrp_dh_NADP.
[Graphical view]
PfamiPF16653. Sacchrp_dh_C. 1 hit.
PF03435. Sacchrp_dh_NADP. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

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)DescriptionActionsGraphical viewLength
Natural varianti140E → G in strain: 4091-5-8. 1
Natural varianti398L → F in strain: 4091-5-8. 1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:MGG_17041.

Phylogenomic databases

InParanoidiQ9P4R4.
KOiK00293.
OrthoDBiEOG092C2J3O.

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.
IPR032095. Sacchrp_dh_C.
IPR005097. Sacchrp_dh_NADP.
[Graphical view]
PfamiPF16653. Sacchrp_dh_C. 1 hit.
PF03435. Sacchrp_dh_NADP. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

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 30, 2016
This is version 111 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

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 one 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.