ID   A0A0F0IHS3_ASPPU        Unreviewed;       459 AA.
AC   A0A0F0IHS3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:KJK66726.1};
GN   ORFNames=P875_00127905 {ECO:0000313|EMBL:KJK66726.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66726.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK66726.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJK66726.1}.
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DR   EMBL; JZEE01000233; KJK66726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IHS3; -.
DR   STRING; 1403190.A0A0F0IHS3; -.
DR   Proteomes; UP000033540; 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:UP000033540};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..459
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002443264"
FT   DOMAIN          10..124
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          128..451
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   459 AA;  49429 MW;  02138E19AF652F6C CRC64;
     MSSAIGKKAL LLGAGFVCEP AVQALSEAGV KVTVACRTLS VAQALAANYK STTAIALDVA
     NEPENLRAAI SQTDIVISLI PYVHHALVIS AAIRYNKPVV TTSYISPALW ALDDQAKAAG
     ITVLNEIGLD PGIDHLYAVK TIDEVHKAGG QVKAFTSYCG ALPAPENSDN PLGYKFSWSP
     RGGLLALLNS AQWYRDNDIA TVDGKDLMAA ASPQRIFPGF NLVGYPNRDS VGFRDFYNIP
     EAHTVFRGTL RYAGFPEIIR ALVSIGYFSQ ERMAALERSG ITWVQLTASL LGLSESSSPT
     DVQNAVRRKI EAFITDKDDV DRALSGLRWI GLFDPTPVVG HGTPLDTLCA VLETRMAYQP
     GERDMIVLQH IFDIEHADGS VEKRSSTLVE YGEPLGPGYR SAMAKLVGLP CAVGVLAVLE
     GRIPATGMVA PWSSAEIASL LREELKDKFG IELKERVIT
//