LYS9_MAGO7
ID LYS9_MAGO7 Reviewed; 450 AA.
AC Q9P4R4; A4QYG4; G4N642;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Saccharopine dehydrogenase [NADP(+), L-glutamate-forming];
DE EC=1.5.1.10;
DE AltName: Full=Saccharopine reductase;
GN Name=LYS3; ORFNames=MGG_08564;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION.
RC STRAIN=4091-5-8;
RX PubMed=10771443; DOI=10.1107/s0907444900003735;
RA Johansson E., Steffens J.J., Emptage M., Lindqvist Y., Schneider G.;
RT "Cloning, expression, purification and crystallization of saccharopine
RT reductase from Magnaporthe grisea.";
RL Acta Crystallogr. D 56:662-664(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [3] {ECO:0007744|PDB:1E5L, ECO:0007744|PDB:1E5Q, ECO:0007744|PDB:1FF9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L-SACCHAROPINE AND
RP NADP.
RX PubMed=11080625; DOI=10.1016/s0969-2126(00)00512-8;
RA Johansson E., Steffens J.J., Lindqvist Y., Schneider G.;
RT "Crystal structure of saccharopine reductase from Magnaporthe grisea, an
RT enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.";
RL Structure 8:1037-1047(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NADP(+) = (S)-2-amino-6-oxohexanoate +
CC H(+) + L-glutamate + NADPH; Xref=Rhea:RHEA:10020, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57951, ChEBI:CHEBI:58321, ChEBI:CHEBI:58349; EC=1.5.1.10;
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 2/3.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF144424; AAF91081.1; -; Genomic_DNA.
DR EMBL; CM001234; EHA49766.1; -; Genomic_DNA.
DR RefSeq; XP_003716085.1; XM_003716037.1.
DR PDB; 1E5L; X-ray; 2.40 A; A/B=1-450.
DR PDB; 1E5Q; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-450.
DR PDB; 1FF9; X-ray; 2.00 A; A=1-450.
DR PDBsum; 1E5L; -.
DR PDBsum; 1E5Q; -.
DR PDBsum; 1FF9; -.
DR AlphaFoldDB; Q9P4R4; -.
DR SMR; Q9P4R4; -.
DR STRING; 318829.MGG_17041T0; -.
DR PRIDE; Q9P4R4; -.
DR EnsemblFungi; MGG_17041T0; MGG_17041T0; MGG_17041.
DR GeneID; 12984319; -.
DR KEGG; mgr:MGG_17041; -.
DR VEuPathDB; FungiDB:MGG_17041; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_016207_3_1_1; -.
DR InParanoid; Q9P4R4; -.
DR OMA; WNYKFTW; -.
DR OrthoDB; 535756at2759; -.
DR BRENDA; 1.5.1.10; 5238.
DR UniPathway; UPA00033; UER00033.
DR EvolutionaryTrace; Q9P4R4; -.
DR Proteomes; UP000009058; Chromosome 4.
DR GO; GO:0004755; F:saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Lysine biosynthesis; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..450
FT /note="Saccharopine dehydrogenase [NADP(+), L-glutamate-
FT forming]"
FT /id="PRO_0000212838"
FT BINDING 11..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 55..56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 98..99
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 99..100
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 125..127
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 126
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 224
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT BINDING 245..247
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:11080625,
FT ECO:0007744|PDB:1E5Q"
FT VARIANT 140
FT /note="E -> G (in strain: 4091-5-8)"
FT VARIANT 398
FT /note="L -> F (in strain: 4091-5-8)"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1FF9"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:1FF9"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1E5Q"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1FF9"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 147..159
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1E5Q"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 239..248
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:1FF9"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:1FF9"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1E5Q"
FT HELIX 336..347
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 356..367
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 373..383
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 394..411
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1FF9"
FT HELIX 426..440
FT /evidence="ECO:0007829|PDB:1FF9"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:1FF9"
SQ SEQUENCE 450 AA; 49097 MW; 9997B94CF1245035 CRC64;
MATKSVLMLG SGFVTRPTLD VLTDSGIKVT VACRTLESAK KLSAGVQHST PISLDVNDDA
ALDAEVAKHD LVISLIPYTF HATVIKSAIR QKKHVVTTSY VSPAMMELDQ AAKDAGITVM
NEIGLDPGID HLYAIKTIEE VHAAGGKIKT FLSYCGGLPA PESSDNPLGY KFSWSSRGVL
LALRNAASFY KDGKVTNVAG PELMATAKPY FIYPGFAFVA YPNRDSTPYK ERYQIPEADN
IVRGTLRYQG FPQFIKVLVD IGFLSDEEQP FLKEAIPWKE ATQKIVKASS ASEQDIVSTI
VSNATFESTE EQKRIVAGLK WLGIFSDKKI TPRGNALDTL CATLEEKMQF EEGERDLVML
QHKFEIENKD GSRETRTSSL CEYGAPIGSG GYSAMAKLVG VPCAVAVKFV LDGTISDRGV
LAPMNSKIND PLMKELKEKY GIECKEKVVA
