EzCatDB: T00219
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DB codeT00219
CATH domainDomain 13.40.50.720 : Rossmann fold
Domain 23.30.360.10 : Dihydrodipicolinate Reductase; domain 2Catalytic domain
Domain 31.10.1870.10 : Domain 3, Saccharopine reductase
E.C.1.5.1.10
CSA1e5q

CATH domainRelated DB codes (homologues)
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2D00003,D00010,D00017,D00023,D00027,D00028,D00034,D00476
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

Q9P4R4
Protein nameSaccharopine dehydrogenase {NADP+, L-glutamate-forming}saccharopine dehydrogenase (NADP+, L-glutamate-forming)
saccharopine (nicotinamide adenine dinucleotide phosphate,glutamate-forming) dehydrogenase
aminoadipic semialdehyde-glutamic reductase
aminoadipate semialdehyde-glutamate reductase
aminoadipic semialdehyde-glutamate reductase
epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase(L-2-aminoadipate-semialdehyde forming)
saccharopine reductase
6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase(L-glutamate-forming)
SynonymsEC 1.5.1.10
Saccharopine reductase
RefSeqXP_003716085.1 (Protein)
XM_003716037.1 (DNA/RNA sequence)
PfamPF03435 (Saccharop_dh)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00300Lysine biosynthesis
MAP00310Lysine degradation

UniProtKB:Accession NumberQ9P4R4
Entry nameLYS9_MAGGR
ActivityN(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00005C00025C04076C00080C00006C00449C00001
CompoundNADPHL-GlutamateL-2-Aminoadipate 6-semialdehydeH+NADP+N6-(L-1,3-Dicarboxypropyl)-L-lysineH2O
Typeamide group,amine group,nucleotideamino acids,carboxyl groupamino acids,carbohydrate,lipidothersamide group,amine group,nucleotideamino acids,amine group,carboxyl groupH2O
ChEBI16474
16015
17917
58321
15378
18009
16927
15377
PubChem5884
88747398
44272391
33032
36688062
160603
1038
5886
160556
962
22247451
               
1e5lA01UnboundUnboundUnbound UnboundUnbound 
1e5lB01UnboundUnboundUnbound UnboundUnbound 
1e5qA01UnboundUnboundUnbound UnboundUnbound 
1e5qB01UnboundUnboundUnbound UnboundUnbound 
1e5qC01UnboundUnboundUnbound UnboundUnbound 
1e5qD01UnboundUnboundUnbound UnboundUnbound 
1e5qE01UnboundUnboundUnbound UnboundUnbound 
1e5qF01UnboundUnboundUnbound UnboundUnbound 
1e5qG01UnboundUnboundUnbound UnboundUnbound 
1e5qH01UnboundUnboundUnbound UnboundUnbound 
1ff9A01UnboundUnboundUnbound UnboundUnbound 
1e5lA02UnboundUnboundUnbound UnboundUnbound 
1e5lB02UnboundUnboundUnbound UnboundUnbound 
1e5qA02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qB02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qC02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qD02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qE02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qF02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qG02Bound:NDPUnboundUnbound UnboundBound:SHR 
1e5qH02Bound:NDPUnboundUnbound UnboundBound:SHR 
1ff9A02UnboundUnboundUnbound UnboundUnbound 
1e5lA03UnboundUnboundUnbound UnboundUnbound 
1e5lB03UnboundUnboundUnbound UnboundUnbound 
1e5qA03UnboundUnboundUnbound UnboundUnbound 
1e5qB03UnboundUnboundUnbound UnboundUnbound 
1e5qC03UnboundUnboundUnbound UnboundUnbound 
1e5qD03UnboundUnboundUnbound UnboundUnbound 
1e5qE03UnboundUnboundUnbound UnboundUnbound 
1e5qF03UnboundUnboundUnbound UnboundUnbound 
1e5qG03UnboundUnboundUnbound UnboundUnbound 
1e5qH03UnboundUnboundUnbound UnboundUnbound 
1ff9A03UnboundUnboundUnbound UnboundUnbound 

Active-site residues
resource
literature [3]
pdbCatalytic residues
         
1e5lA01 
1e5lB01 
1e5qA01 
1e5qB01 
1e5qC01 
1e5qD01 
1e5qE01 
1e5qF01 
1e5qG01 
1e5qH01 
1ff9A01 
1e5lA02ASP 126
1e5lB02ASP 126
1e5qA02ASP 126
1e5qB02ASP 126
1e5qC02ASP 126
1e5qD02ASP 126
1e5qE02ASP 126
1e5qF02ASP 126
1e5qG02ASP 126
1e5qH02ASP 126
1ff9A02ASP 126
1e5lA03 
1e5lB03 
1e5qA03 
1e5qB03 
1e5qC03 
1e5qD03 
1e5qE03 
1e5qF03 
1e5qG03 
1e5qH03 
1ff9A03 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.7, p.1042-10443

references
[1]
PubMed ID242268
JournalArch Biochem Biophys
Year1975
Volume171
Pages191-6
AuthorsFjellstedt TA, Robinson JC
TitleProperties of partially purified saccharopine dehydrogenase from human placenta.
[2]
PubMed ID10587945
JournalMicrob Comp Genomics
Year1999
Volume4
Pages173-86
AuthorsStudley WK, Yamaguchi M, Hatefi Y, Saier MH Jr
TitlePhylogenetic analyses of proton-translocating transhydrogenases.
[3]
CommentsX-ray crystallography
PubMed ID11080625
JournalStructure Fold Des
Year2000
Volume8
Pages1037-47
AuthorsJohansson E, Steffens JJ, Lindqvist Y, Schneider G
TitleCrystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.
Related PDB1e5l,1e5q,1ffq
[4]
PubMed ID12393892
JournalJ Biol Chem
Year2002
Volume277
Pages49655-61
AuthorsZhu X, Tang G, Galili G
TitleThe activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains.

comments
Saccharopine Dehydrogenases are a collective term for the enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-lysine, or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-glutamate.
According to the paper [3], this enzyme catalyzes three different reactions, addition to double-bond, elimination accompanied by double-bond formation, and reduction.

createdupdated
2004-07-022009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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