LYS1_SCHPO
ID LYS1_SCHPO Reviewed; 368 AA.
AC Q09694; Q9UTC1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming];
DE Short=SDH;
DE EC=1.5.1.7;
DE AltName: Full=Lysine--2-oxoglutarate reductase;
GN Name=lys3 {ECO:0000303|PubMed:3142867};
GN ORFNames=SPAC227.18 {ECO:0000312|PomBase:SPAC227.18}, SPAC2F7.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=3142867; DOI=10.1128/jb.170.12.5968-5970.1988;
RA Ye Z.H., Bhattacharjee J.K.;
RT "Lysine biosynthesis pathway and biochemical blocks of lysine auxotrophs of
RT Schizosaccharomyces pombe.";
RL J. Bacteriol. 170:5968-5970(1988).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-
CC lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate
CC (AAA) pathway for lysin biosynthesis. {ECO:0000250|UniProtKB:P38998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-
CC lysine + NADH; Xref=Rhea:RHEA:12440, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57951; EC=1.5.1.7;
CC Evidence={ECO:0000250|UniProtKB:P38998};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
CC {ECO:0000305|PubMed:3142867}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38998}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; CU329670; CAB61467.1; -; Genomic_DNA.
DR PIR; T38549; S58145.
DR PIR; T50174; T50174.
DR RefSeq; NP_592972.1; NM_001018372.2.
DR AlphaFoldDB; Q09694; -.
DR SMR; Q09694; -.
DR BioGRID; 278002; 38.
DR IntAct; Q09694; 4.
DR MINT; Q09694; -.
DR STRING; 4896.SPAC227.18.1; -.
DR iPTMnet; Q09694; -.
DR MaxQB; Q09694; -.
DR PaxDb; Q09694; -.
DR PRIDE; Q09694; -.
DR EnsemblFungi; SPAC227.18.1; SPAC227.18.1:pep; SPAC227.18.
DR GeneID; 2541500; -.
DR KEGG; spo:SPAC227.18; -.
DR PomBase; SPAC227.18; lys3.
DR VEuPathDB; FungiDB:SPAC227.18; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_063085_0_0_1; -.
DR InParanoid; Q09694; -.
DR OMA; YFFFSHT; -.
DR PhylomeDB; Q09694; -.
DR UniPathway; UPA00033; UER00034.
DR PRO; PR:Q09694; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; ISO:PomBase.
DR GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009085; P:lysine biosynthetic process; IMP:PomBase.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:PomBase.
DR CDD; cd12188; SDH; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR027281; Lys1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR PIRSF; PIRSF018250; Saccharopine_DH_Lys; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Disulfide bond; Lysine biosynthesis; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..368
FT /note="Saccharopine dehydrogenase [NAD(+), L-lysine-
FT forming]"
FT /id="PRO_0000199014"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 18
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 77
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 101
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 131
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 135
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 279..281
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 319..322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT DISULFID 205..249
FT /evidence="ECO:0000250|UniProtKB:P38998"
SQ SEQUENCE 368 AA; 41393 MW; 789AB01DB171ED13 CRC64;
MVAPHLWLRA ETKPLEERSA LTPRTAKILA DAGFQITIER SSQRAFKDKE FERLGFPMVP
EGSWRHAPKD AYIIGLKELP ENDNSPLKHT HIQFAHCYKN QEGWREVLSR FPAGNGLLYD
LEFLQDDNGR RVAAFGYHAG FAGSAISCLV WAHQLLHPNK QFPAIRPFPN EKSLVRHVAR
QVRLALKKNN NQYPRILVIG ALGRCGTGAC DLASKIGIPF DNILRWDINE TKKGGPFTEI
TESDIFVNCI YLSMPIPKFC TVESLNVPNR KLRVVCDVSC DTTNPNNPIP IYNVNTTFDH
PTVEVKGVTT PPPLEVISID HLPTLLPRES SEAFSEALIP SLLALKDVDN APVWVRAKKL
YETMVQKL
