LYS9_SCHPO
ID LYS9_SCHPO Reviewed; 450 AA.
AC O59711;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Saccharopine dehydrogenase [NADP(+), L-glutamate-forming];
DE EC=1.5.1.10;
DE AltName: Full=Saccharopine reductase;
GN Name=lys9 {ECO:0000250|UniProtKB:P38999}; ORFNames=SPBC3B8.03;
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] {ECO:0000312|EMBL:CAA18292.1}
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] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. {ECO:0000250|UniProtKB:Q9P4R4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; CU329671; CAA18292.1; -; Genomic_DNA.
DR PIR; T40337; T40337.
DR RefSeq; NP_596411.1; NM_001022330.2.
DR AlphaFoldDB; O59711; -.
DR SMR; O59711; -.
DR BioGRID; 277424; 7.
DR STRING; 4896.SPBC3B8.03.1; -.
DR iPTMnet; O59711; -.
DR MaxQB; O59711; -.
DR PaxDb; O59711; -.
DR PRIDE; O59711; -.
DR EnsemblFungi; SPBC3B8.03.1; SPBC3B8.03.1:pep; SPBC3B8.03.
DR GeneID; 2540908; -.
DR KEGG; spo:SPBC3B8.03; -.
DR PomBase; SPBC3B8.03; lys9.
DR VEuPathDB; FungiDB:SPBC3B8.03; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_016207_3_1_1; -.
DR InParanoid; O59711; -.
DR OMA; WNYKFTW; -.
DR PhylomeDB; O59711; -.
DR Reactome; R-SPO-71064; Lysine catabolism.
DR UniPathway; UPA00033; UER00033.
DR PRO; PR:O59711; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004755; F:saccharopine dehydrogenase (NADP+, L-glutamate-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; IBA:GO_Central.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lysine biosynthesis; NADP;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..450
FT /note="Saccharopine dehydrogenase [NADP(+), L-glutamate-
FT forming]"
FT /id="PRO_0000316856"
FT BINDING 9..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 32..34
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"
SQ SEQUENCE 450 AA; 49938 MW; 1AEE17A423715C71 CRC64;
MPSILLLGSG FVAHPTLEYL SRRKENNITV ACRTLSKAEA FINGIPNSKA IALDVNDEAA
LEKAVSEHDL TISLIPYTYH ATVMKAAIKH GKHVCTTSYV NPKMAELEEA AIKAGSICMN
EIGVDPGIDH LYAIKTIEEV HKAGGKIKSF LSYCGGLPAP EDSNNPLGYK FSWSSRGVLL
ALRNSAKFYE NGKLVEIDGK DLMETAKPYF IYPGYAFVCY PNRDSTVYQE RYQIPEAETI
IRGTLRYQGF PEFIHCLVDM GFLDETAQEY LSPEAPALPW KEVTARVIKA ESSSEADLIK
KISSIHKFKD EDDKKRILNG LKWLGMFSSK PVTPRGNPLD TLCATLEELM QYEEGERDML
ILQHKFEVET KEGKRQTRTC TLLDYGVPNG YTSMAKLVGV PCGVATQQIL DGVINTPGVL
APNDMKLCGP LIDTLAKEGI RLEEEIIDEE
