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Database: UniProt
Entry: A0A2I2GEA0_9EURO
LinkDB: A0A2I2GEA0_9EURO
Original site: A0A2I2GEA0_9EURO 
ID   A0A2I2GEA0_9EURO        Unreviewed;       414 AA.
AC   A0A2I2GEA0;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:PLB51228.1};
GN   ORFNames=P170DRAFT_509250 {ECO:0000313|EMBL:PLB51228.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB51228.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB51228.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB51228.1,
RC   ECO:0000313|Proteomes:UP000234275};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00038048}.
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:PLB51228.1}.
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DR   EMBL; MSFO01000003; PLB51228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2GEA0; -.
DR   VEuPathDB; FungiDB:P170DRAFT_509250; -.
DR   OrthoDB; 5479972at2759; -.
DR   Proteomes; UP000234275; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR12286:SF5; SACCHAROPINE DEHYDROGENASE-LIKE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR12286; UNCHARACTERIZED; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        281..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..139
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
SQ   SEQUENCE   414 AA;  45454 MW;  638BDA54A974AD93 CRC64;
     MQSSREFDLV VLGPTGYTGK LCAEHIVRNL PTNLKWALAG RSVPKIENVA QEIQPLNPDR
     TPPEILAVQL NREELHNLAQ RTKLIINCIG PYVLYSVPVV EACASNGTHY IDATGEPPFI
     KSVLEKYHDT AKATGAIIIP FMGVESAPAD MLSWSLVKRV REELSCHTKE VTCSIDELKS
     SGASGGTLST VLTLFDAVPY PELAKSLKPF ALAASPPPKT LPRESITEKL FGVRCIPDMG
     VLATSPTAIA DIIIVHRSST LMPEFYGPKF TFRQFVRVRN VLVGVALHFI FLIAVSLLVL
     PPVRMLVKQF IYMPGTGPRM EDSTRDRVQY RAVATADQDV QEPKRALGTL KYQGSLYAMT
     GLLMAQGAMV ILENEEKVRK VSRGGIVTPA SLGQEYADRL EAAGCYIETK ILEF
//
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