Reviewed, UniProtKB/Swiss-Prot Q9P4R4 (LYS9_MAGGR)

Names and origin

Protein names

Recommended name:
    Saccharopine dehydrogenase [NADP+, L-glutamate-forming]
    EC=1.5.1.10
Alternative name(s):
    Saccharopine reductase

Gene names

Name:	LYS3
ORF Names:	MGG_08564

Organism

Magnaporthe grisea (Rice blast fungus) (Pyricularia grisea) [Complete proteome]

Taxonomic identifier

148305 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Magnaporthales › Magnaporthaceae › Magnaporthe

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	N(6)-(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 structure	Homodimer.
Sequence similarities	Belongs to the saccharopine dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Lysine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Saccharopine dehydrogenase [NADP+, L-glutamate-forming]

PRO_0000212838

Experimental info

Sequence conflict

140

1

E → G in AAF91081. Ref.1

Sequence conflict

398

1

L → F in AAF91081. Ref.1

Secondary structure

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450

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Helix

15 – 24

10

Beta strand

28 – 35

8

Helix

36 – 43

8

Beta strand

49 – 53

5

Helix

59 – 67

9

Beta strand

69 – 74

6

Helix

78 – 80

3

Helix

81 – 90

10

Beta strand

94 – 99

6

Helix

103 – 107

5

Helix

109 – 114

6

Beta strand

118 – 120

3

Turn

125 – 127

3

Helix

129 – 144

16

Beta strand

147 – 159

13

Helix

161 – 163

3

Beta strand

172 – 174

3

Turn

177 – 181

5

Helix

182 – 184

3

Beta strand

187 – 191

5

Beta strand

194 – 198

5

Helix

200 – 202

3

Helix

204 – 206

3

Beta strand

218 – 222

5

Helix

229 – 232

4

Beta strand

239 – 248

10

Helix

251 – 260

10

Turn

261 – 264

4

Helix

271 – 273

3

Helix

278 – 286

9

Beta strand

289 – 292

4

Helix

293 – 303

11

Helix

309 – 322

14

Turn

323 – 325

3

Beta strand

326 – 329

4

Helix

336 – 347

12

Beta strand

356 – 367

12

Beta strand

373 – 383

11

Helix

394 – 411

18

Beta strand

419 – 421

3

Helix

426 – 438

13

Beta strand

445 – 448

4

Sequences

	Sequence		Length	Mass (Da)
	Q9P4R4-1 [UniParc]. Last modified June 12, 2007. Version 2. Checksum: 9997B94CF1245035	FASTA	450	49,097
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(2000) [PubMed: 10771443] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CRYSTALLIZATION. Strain: 4091-5-8.
[2]	"The genome sequence of the rice blast fungus Magnaporthe grisea." 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. Nature 434:980-986(2005) [PubMed: 15846337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 70-15 / 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(2000) [PubMed: 11080625] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF144424 Genomic DNA. Translation: AAF91081.1.
CH476827 Genomic DNA. Translation: EDJ97077.1.

RefSeq

XP_362873.1.

UniGene

Mgr.12109

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E5L	X-ray	2.40	A/B	1-450	[»]
1E5Q	X-ray	2.10	A/B/C/D/E/F/G/H	1-450	[»]
1FF9	X-ray	2.00	A	1-450	[»]

ModBase

Search...

Genome annotation databases

GeneID

2678741.

KEGG

mgr:MGG_08564.

NMPDR

fig|242507.1.peg.4613.

Phylogenomic databases

OMA

Q9P4R4. PYFIYPG.

Enzyme and pathway databases

BRENDA

1.5.1.10. 5953.

Family and domain databases

InterPro

IPR016040. NAD(P)-bd_dom.
IPR005097. Saccharopine_DH.
[Graphical view]

Gene3D

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

Pfam

PF03435. Saccharop_dh. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LYS9_MAGGR

Accession

Primary (citable) accession number: Q9P4R4
Secondary accession number(s): A4QYG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	June 12, 2007
Last modified:	June 16, 2009
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)