LYS9_YEAST
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 03-AUG-2022, entry version 177.
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; 23.
DR DIP; DIP-776N; -.
DR IntAct; P38999; 9.
DR MINT; P38999; -.
DR STRING; 4932.YNR050C; -.
DR iPTMnet; P38999; -.
DR MaxQB; P38999; -.
DR PaxDb; P38999; -.
DR PRIDE; P38999; -.
DR EnsemblFungi; YNR050C_mRNA; YNR050C; YNR050C.
DR GeneID; 855786; -.
DR KEGG; sce:YNR050C; -.
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 BioCyc; YEAST:MON3O-363; -.
DR BRENDA; 1.5.1.10; 984.
DR Reactome; R-SCE-71064; Lysine catabolism.
DR UniPathway; UPA00033; UER00033.
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 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; 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
