ID   A0A319DQV0_9EURO        Unreviewed;       449 AA.
AC   A0A319DQV0;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 10.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:PYH99839.1};
GN   ORFNames=BO71DRAFT_393808 {ECO:0000313|EMBL:PYH99839.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH99839.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH99839.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH99839.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ825798; PYH99839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319DQV0; -.
DR   STRING; 1448320.A0A319DQV0; -.
DR   Proteomes; UP000247810; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
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   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810}.
FT   DOMAIN          6..120
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          124..441
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   449 AA;  48867 MW;  35C3FE0430AFCDE3 CRC64;
     MASHSVLMLG AGFVTRPTLD ILSESGIPVT VACRTIESAK ALSAGVKLAT PISLDVTNDQ
     ALDAEVAKHS LVISLIPYTF HATVIKSAIR QKKHVVTTSY VSPAMLELDQ QCKDAGITVM
     NEIGLDPGID HLYAVKTIEE VHKEGGKITS FLSYCGGLPA PENSGNPLGY KFSWSPRGVL
     LALRNAASFY KDGKVVNVAG PDLMATAKPY HIYPGYALVA YPNRDSTPYK ERYNIPEAQT
     IIRGTLRYGG FPEFVKVLVD IGFLKDEEQS FLKEPISWKE ATQKVLGATS SDEKDLVEAI
     AYKTTFADNA QRDHLLAGLK WVGLFSDEKI LPRGNPLDTI CATLEKKMQF AEGERDLVIL
     QHKFEVELKD GTKQTRTSTL VEYGSTEPSG YSAMAKLVGV PCAVAVKQVL NGTIAEKGVL
     APMNSKLNDP LIKELKEKYG IACKEEIVA
//