ID   A0A1V8T082_9PEZI        Unreviewed;       462 AA.
AC   A0A1V8T082;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] {ECO:0000313|EMBL:OQO04618.1};
GN   ORFNames=B0A48_09540 {ECO:0000313|EMBL:OQO04618.1};
OS   Rachicladosporium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO04618.1, ECO:0000313|Proteomes:UP000192596};
RN   [1] {ECO:0000313|Proteomes:UP000192596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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:OQO04618.1}.
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DR   EMBL; NAJO01000021; OQO04618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8T082; -.
DR   STRING; 1507870.A0A1V8T082; -.
DR   InParanoid; A0A1V8T082; -.
DR   OrthoDB; 2184985at2759; -.
DR   Proteomes; UP000192596; 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:UP000192596}.
FT   DOMAIN          13..126
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          131..454
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   462 AA;  50803 MW;  031995D58DE7CA80 CRC64;
     MDTILTSKRG QYVLLLGAGF VTRPTAVELD KLGVNITVAC RTLASAQKLS EGLSHATPIS
     LDVNDLEALE KEIEKNDLVI SLIPYTFHAA VIKAAIKMKK HVVTTSYVSD EMRALNQDCI
     NAGITCFNEI GLDPGIDHLY AVKTISEVHE AGGKITGFLS YCGGLPAPEN SDNPLGYKFS
     WSPRGVLLAA RNTGVYYENG EKKTTPGSEL MSTAKPYRIY PGYAFEAYPN RDSTPFRERY
     NIPEAQLLIR GTLRYQGAPA FIQKLTDLGF LSTDEIDILK KTSTEPPTWA EAFAKILGAS
     SHSEADLVLA VAGKTSFKDE EERNQIIAGL RWIGVFSSTE RIEPRSTPLD VLCASLEKKM
     QYEKGERDMV MLQHKFFIEW ADGKEETRTS TLVEYGEPEG SGGYSAMAKL VGVPCAVAVK
     MVLDGEIKDR GVLAPVTPEL SEPIRINLKE QYGIELTEKS EL
//