ID   LYS9_YEAST              Reviewed;         446 AA.
AC   P38999; D6W1M5; E9P930;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Saccharopine dehydrogenase [NADP(+), L-glutamate-forming];
DE            EC=1.5.1.10;
DE   AltName: Full=Saccharopine reductase;
GN   Name=LYS9; Synonyms=LYS13; OrderedLocusNames=YNR050C; ORFNames=N3461;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1278B;
RA   Feller A.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 314-324.
RC   STRAIN=ATCC 38531 / Y41;
RX   PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA   Norbeck J., Blomberg A.;
RT   "Protein expression during exponential growth in 0.7 M NaCl medium of
RT   Saccharomyces cerevisiae.";
RL   FEMS Microbiol. Lett. 137:1-8(1996).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   INTERACTION WITH TRM112.
RX   PubMed=15899842; DOI=10.1128/mcb.25.11.4359-4370.2005;
RA   Purushothaman S.K., Bujnicki J.M., Grosjean H., Lapeyre B.;
RT   "Trm11p and Trm112p are both required for the formation of 2-
RT   methylguanosine at position 10 in yeast tRNA.";
RL   Mol. Cell. Biol. 25:4359-4370(2005).
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: Interacts with TRM112. {ECO:0000269|PubMed:15899842}.
CC   -!- MISCELLANEOUS: Present with 57500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X77363; CAA54552.1; -; Genomic_DNA.
DR   EMBL; Z71665; CAA96331.1; -; Genomic_DNA.
DR   EMBL; AY693210; AAT93229.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10591.1; -; Genomic_DNA.
DR   PIR; S41937; S41937.
DR   RefSeq; NP_014448.1; NM_001183227.1.
DR   PDB; 2AXQ; X-ray; 1.70 A; A=1-446.
DR   PDBsum; 2AXQ; -.
DR   AlphaFoldDB; P38999; -.
DR   SMR; P38999; -.
DR   BioGRID; 35875; 30.
DR   DIP; DIP-776N; -.
DR   IntAct; P38999; 9.
DR   MINT; P38999; -.
DR   STRING; 4932.YNR050C; -.
DR   iPTMnet; P38999; -.
DR   MaxQB; P38999; -.
DR   PaxDb; 4932-YNR050C; -.
DR   PeptideAtlas; P38999; -.
DR   EnsemblFungi; YNR050C_mRNA; YNR050C; YNR050C.
DR   GeneID; 855786; -.
DR   KEGG; sce:YNR050C; -.
DR   AGR; SGD:S000005333; -.
DR   SGD; S000005333; LYS9.
DR   VEuPathDB; FungiDB:YNR050C; -.
DR   eggNOG; KOG0172; Eukaryota.
DR   GeneTree; ENSGT00940000176061; -.
DR   HOGENOM; CLU_016207_3_1_1; -.
DR   InParanoid; P38999; -.
DR   OMA; WNYKFTW; -.
DR   OrthoDB; 2184985at2759; -.
DR   BioCyc; YEAST:MONOMER3O-363; -.
DR   BRENDA; 1.5.1.10; 984.
DR   Reactome; R-SCE-71064; Lysine catabolism.
DR   UniPathway; UPA00033; UER00033.
DR   BioGRID-ORCS; 855786; 2 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P38999; -.
DR   PRO; PR:P38999; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P38999; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004755; F:saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity; IDA:SGD.
DR   GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:SGD.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Direct protein sequencing;
KW   Lysine biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..446
FT                   /note="Saccharopine dehydrogenase [NADP(+), L-glutamate-
FT                   forming]"
FT                   /id="PRO_0000212839"
FT   BINDING         10..13
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         33..35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         54..55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         75
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         97..98
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         98..99
FT                   /ligand="L-saccharopine"
FT                   /ligand_id="ChEBI:CHEBI:57951"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         124..126
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         125
FT                   /ligand="L-saccharopine"
FT                   /ligand_id="ChEBI:CHEBI:57951"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         174
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         223
FT                   /ligand="L-saccharopine"
FT                   /ligand_id="ChEBI:CHEBI:57951"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   BINDING         244..246
FT                   /ligand="L-saccharopine"
FT                   /ligand_id="ChEBI:CHEBI:57951"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT   CONFLICT        393
FT                   /note="A -> T (in Ref. 4; AAT93229)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           14..22
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          27..35
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           36..43
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   TURN            44..47
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           58..66
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           80..90
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           102..114
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           128..142
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          146..158
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           176..180
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          217..221
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          238..247
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           250..259
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   TURN            260..263
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           269..271
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           277..285
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          288..291
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           292..300
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           308..320
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   TURN            321..324
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           335..346
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          355..366
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          372..382
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           390..407
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          414..417
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   HELIX           422..436
FT                   /evidence="ECO:0007829|PDB:2AXQ"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:2AXQ"
SQ   SEQUENCE   446 AA;  48918 MW;  1EC4CE1CE3BCD916 CRC64;
     MGKNVLLLGS GFVAQPVIDT LAANDDINVT VACRTLANAQ ALAKPSGSKA ISLDVTDDSA
     LDKVLADNDV VISLIPYTFH PNVVKSAIRT KTDVVTSSYI SPALRELEPE IVKAGITVMN
     EIGLDPGIDH LYAVKTIDEV HRAGGKLKSF LSYCGGLPAP EDSDNPLGYK FSWSSRGVLL
     ALRNSAKYWK DGKIETVSSE DLMATAKPYF IYPGYAFVCY PNRDSTLFKD LYHIPEAETV
     IRGTLRYQGF PEFVKALVDM GMLKDDANEI FSKPIAWNEA LKQYLGAKST SKEDLIASID
     SKATWKDDED RERILSGFAW LGLFSDAKIT PRGNALDTLC ARLEELMQYE DNERDMVVLQ
     HKFGIEWADG TTETRTSTLV DYGKVGGYSS MAATVGYPVA IATKFVLDGT IKGPGLLAPY
     SPEINDPIMK ELKDKYGIYL KEKTVA
//