ID   SCPDH_DICDI             Reviewed;         480 AA.
AC   Q54NG9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Probable saccharopine dehydrogenase [NADP(+), L-glutamate-forming];
DE            EC=1.5.1.10;
DE   AltName: Full=Saccharopine reductase;
GN   Name=sdh; ORFNames=DDB_G0285267;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17259634; DOI=10.1099/mic.0.2006/000562-0;
RA   Serafimidis I., Bloomfield G., Skelton J., Ivens A., Kay R.R.;
RT   "A new environmentally resistant cell type from Dictyostelium.";
RL   Microbiology 153:619-630(2007).
RN   [3]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA   Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA   Skelton J., Ivens A., Bozzaro S.;
RT   "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT   bacteria in Dictyostelium.";
RL   BMC Genomics 9:291-291(2008).
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   -!- DEVELOPMENTAL STAGE: Up-regulated in aspidocytes, environmentally
CC       resistant cell types. {ECO:0000269|PubMed:17259634}.
CC   -!- INDUCTION: Down-regulated by phagocytic stimuli.
CC       {ECO:0000269|PubMed:18559084}.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000077; EAL64797.1; -; Genomic_DNA.
DR   RefSeq; XP_638300.1; XM_633208.1.
DR   AlphaFoldDB; Q54NG9; -.
DR   SMR; Q54NG9; -.
DR   STRING; 44689.Q54NG9; -.
DR   PaxDb; 44689-DDB0238270; -.
DR   EnsemblProtists; EAL64797; EAL64797; DDB_G0285267.
DR   GeneID; 8625017; -.
DR   KEGG; ddi:DDB_G0285267; -.
DR   dictyBase; DDB_G0285267; sdh.
DR   eggNOG; KOG0172; Eukaryota.
DR   HOGENOM; CLU_016207_3_1_1; -.
DR   InParanoid; Q54NG9; -.
DR   OMA; WNYKFTW; -.
DR   PhylomeDB; Q54NG9; -.
DR   Reactome; R-DDI-71064; Lysine catabolism.
DR   UniPathway; UPA00033; UER00033.
DR   PRO; PR:Q54NG9; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004755; F:saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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; SACCHAROPINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..480
FT                   /note="Probable saccharopine dehydrogenase [NADP(+), L-
FT                   glutamate-forming]"
FT                   /id="PRO_0000365593"
SQ   SEQUENCE   480 AA;  53359 MW;  10EE7E6746F7F894 CRC64;
     MKNILLLGSG FVAKPALDYL LKREDYFVTI VSLFQNELDS ITKGHDTSKF KTIQLDVMNK
     LNELEEYFPK SDCVISLIPA TLHSTVAKLC IKHKTHLVTA SYISDDMKAL SEEAKEAGVL
     LLNELGLDPG IDHMSSMKII DHAKENGGKV TSFVSWCGAL PSTECADNPF GYKFSWSPRG
     VLSSATLSAN FLWEGHNEEV PANIKWAVLQ PIVVEDSNGV KMEFDGVPNR NSFPYIEQYN
     LNAKDVTTMF RGTLRWKGGF GIMIRALVAV GLFSTEVDAR LAVEGGISWR NYLVQLLGCN
     DNDSDLLYCV ESTIKEYFEK LKTERDGLQF HFPIIPRDIE KDVQHAVEGF KWLGLLSADE
     KVVNKNTPID SLCALLEKKL SYKAGERDVV VLEHNFVVQY ADRTEKEVSS LICYGIPNGS
     SATSLTVGVP VGIATELIAD GKTTTRGVVG PVTPEFYLPI LEKLKSENIE MIETKQEIKK
//