[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION. STRAIN=4091-5-8; DOI=10.1107/S0907444900003735; PubMed=10771443 [NCBI, ExPASy, EBI, Israel, Japan] Johansson E., Steffens J.J., Emptage M., Lindqvist Y., Schneider G.; "Cloning, expression, purification and crystallization of saccharopine reductase from Magnaporthe grisea."; Acta Crystallogr. D 56:662-664(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=70-15 / FGSC 8958; DOI=10.1038/nature03449; PubMed=15846337 [NCBI, ExPASy, EBI, Israel, Japan] Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K., Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D., Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S., Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M., Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E., Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.; "The genome sequence of the rice blast fungus Magnaporthe grisea."; Nature 434:980-986(2005).
[3]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1016/S0969-2126(00)00512-8; PubMed=11080625 [NCBI, ExPASy, EBI, Israel, Japan] Johansson E., Steffens J.J., Lindqvist Y., Schneider G.; "Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis."; Structure 8:1037-1047(2000).

Comments

CATALYTIC ACTIVITY: N⁶-(L-1,3-dicarboxypropyl)-L-lysine + NADP⁺ + H₂O = L-glutamate + L-2-aminoadipate 6-semialdehyde + NADPH.
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungi route): step 2/3 .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the saccharopine dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF144424; AAF91081.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH476827; EDJ97077.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_362873.1; -.

UniGene

Mgr.12109

3D structure databases

PDB

1E5L; X-ray; 2.40 A; A/B=1-450.	[ExPASy / RCSB / EBI]
1E5Q; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-450.	[ExPASy / RCSB / EBI]
1FF9; X-ray; 2.00 A; A=1-450.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1E5L; -.
1E5Q; -.
1FF9; -.

ModBase

Q9P4R4.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR005097; Saccharopine_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 2.

Pfam

PF03435; Saccharop_dh; 1.
Pfam graphical view of domain structure.

BLOCKS

Q9P4R4.

Genome annotation databases

GeneID

2678741; -.

KEGG

mgr:MGG_08564; -.

NMPDR

fig|242507.1.peg.4613; -.

Other

Q9P4R4; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 450`	`450`	`Saccharopine dehydrogenase [NADP+, L-glutamate-forming].`	`PRO_0000212838`
`CONFLICT`	`140 140`		`E -> G (in Ref. 1; AAF91081).`
`CONFLICT`	`398 398`		`L -> F (in Ref. 1; AAF91081).`
`STRAND`	`5 9`	`5`
`HELIX`	`15 24`	`10`
`STRAND`	`28 35`	`8`
`HELIX`	`36 43`	`8`
`STRAND`	`49 53`	`5`
`HELIX`	`59 67`	`9`
`STRAND`	`69 74`	`6`
`HELIX`	`78 80`	`3`
`HELIX`	`81 90`	`10`
`STRAND`	`94 99`	`6`
`HELIX`	`103 107`	`5`
`HELIX`	`109 114`	`6`
`STRAND`	`118 120`	`3`
`TURN`	`125 127`	`3`
`HELIX`	`129 144`	`16`
`STRAND`	`147 159`	`13`
`HELIX`	`161 163`	`3`
`STRAND`	`172 174`	`3`
`TURN`	`177 181`	`5`
`HELIX`	`182 184`	`3`
`STRAND`	`187 191`	`5`
`STRAND`	`194 198`	`5`
`HELIX`	`200 202`	`3`
`HELIX`	`204 206`	`3`
`STRAND`	`218 222`	`5`
`HELIX`	`229 232`	`4`
`STRAND`	`239 248`	`10`
`HELIX`	`251 260`	`10`
`TURN`	`261 264`	`4`
`HELIX`	`271 273`	`3`
`HELIX`	`278 286`	`9`
`STRAND`	`289 292`	`4`
`HELIX`	`293 303`	`11`
`HELIX`	`309 322`	`14`
`TURN`	`323 325`	`3`
`STRAND`	`326 329`	`4`
`HELIX`	`336 347`	`12`
`STRAND`	`356 367`	`12`
`STRAND`	`373 383`	`11`
`HELIX`	`394 411`	`18`
`STRAND`	`419 421`	`3`
`HELIX`	`426 438`	`13`
`STRAND`	`445 448`	`4`

Sequence information

Length: 450 AA [This is the length of the unprocessed precursor]

Molecular weight: 49097 Da [This is the MW of the unprocessed precursor]

CRC64: 9997B94CF1245035 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATKSVLMLG SGFVTRPTLD VLTDSGIKVT VACRTLESAK KLSAGVQHST PISLDVNDDA 

        70         80         90        100        110        120 
ALDAEVAKHD LVISLIPYTF HATVIKSAIR QKKHVVTTSY VSPAMMELDQ AAKDAGITVM 

       130        140        150        160        170        180 
NEIGLDPGID HLYAIKTIEE VHAAGGKIKT FLSYCGGLPA PESSDNPLGY KFSWSSRGVL 

       190        200        210        220        230        240 
LALRNAASFY KDGKVTNVAG PELMATAKPY FIYPGFAFVA YPNRDSTPYK ERYQIPEADN 

       250        260        270        280        290        300 
IVRGTLRYQG FPQFIKVLVD IGFLSDEEQP FLKEAIPWKE ATQKIVKASS ASEQDIVSTI 

       310        320        330        340        350        360 
VSNATFESTE EQKRIVAGLK WLGIFSDKKI TPRGNALDTL CATLEEKMQF EEGERDLVML 

       370        380        390        400        410        420 
QHKFEIENKD GSRETRTSSL CEYGAPIGSG GYSAMAKLVG VPCAVAVKFV LDGTISDRGV 

       430        440        450 
LAPMNSKIND PLMKELKEKY GIECKEKVVA

Q9P4R4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools