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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: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

N6-(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. no protein annotated in this organism
  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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76NADP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei126SaccharopineCombined sources1 Publication1
Binding sitei175NADP; via amide nitrogenCombined sources1 Publication1
Binding sitei224SaccharopineCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 14NADPCombined sources1 Publication4
Nucleotide bindingi33 – 35NADPCombined sources1 Publication3
Nucleotide bindingi55 – 56NADPCombined sources1 Publication2
Nucleotide bindingi98 – 99NADPCombined sources1 Publication2
Nucleotide bindingi125 – 127NADPCombined sources1 Publication3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Lysine biosynthesis
LigandNADP

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

Proteomic databases

PRIDEiQ9P4R4

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi318829.MGG_17041T0

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Saccharopine bindingCombined sources1 Publication2
Regioni245 – 247Saccharopine bindingCombined sources1 Publication3

Sequence similaritiesi

Belongs to the saccharopine dehydrogenase family.Curated

Phylogenomic databases

InParanoidiQ9P4R4
KOiK00293
OrthoDBiEOG092C2J3O

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR032095 Sacchrp_dh_C
IPR005097 Sacchrp_dh_NADP
PfamiView protein in Pfam
PF16653 Sacchrp_dh_C, 1 hit
PF03435 Sacchrp_dh_NADP, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiLYS9_MAGO7
AccessioniPrimary (citable) accession number: Q9P4R4
Secondary accession number(s): A4QYG4, G4N642
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: June 12, 2007
Last modified: May 23, 2018
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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