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Database: UniProt
Entry: A0A2T9YZ18_9FUNG
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ID   A0A2T9YZ18_9FUNG        Unreviewed;       452 AA.
AC   A0A2T9YZ18;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Saccharopine dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BB559_001968 {ECO:0000313|EMBL:PVU97559.1};
OS   Furculomyces boomerangus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX   NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU97559.1, ECO:0000313|Proteomes:UP000245699};
RN   [1] {ECO:0000313|EMBL:PVU97559.1, ECO:0000313|Proteomes:UP000245699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU97559.1,
RC   ECO:0000313|Proteomes:UP000245699};
RX   PubMed=29764946;
RA   Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT   "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT   Symbiosis.";
RL   MBio 9:e00636-e00618(2018).
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:PVU97559.1}.
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DR   EMBL; MBFT01000104; PVU97559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T9YZ18; -.
DR   STRING; 61424.A0A2T9YZ18; -.
DR   Proteomes; UP000245699; 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:UP000245699}.
FT   DOMAIN          7..122
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          126..445
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   452 AA;  49657 MW;  C16C7E352CBC8244 CRC64;
     MVAQKRILLL GSGFVAGPCV EYLCRRSENI VTIACRGIEK AQNLAKHYPG ALAASVDVQN
     EAELDAAIAQ NDVVISLIPY TYHAQIIKSA IKNKKNVITT SYVSPAMMEL DQQCKDAGII
     CLNEVGLDPG IDHFYALKTI NEVHSNGGKI KSFLSYCGGL PAPEASDNPL GYKFSWSARG
     VLLALLNNAK FWENGQIVQI DGKDLMTSAK PIYINSEFSV VGYPNRDSTN YKERYEIPEA
     ETVLRGTLRY EGFPEFIKAL VDIGYLNGEN QQILSKSNTE PLTWSQLTAN LLGSSSTSSE
     DLLKAIDSKI ITNDSELRAK LIHGMEWLGI VSNDIKVNKK DTYLDTLCAR LEELMQYGPG
     ERDLVILQHK FEIENSNGST ETRTSTMIEY GIPNGNTAMA TTVGVPCGIA TQLVLDGKIT
     QTGVIAPMKP EIYVPIMTEL EKEGIRCVEQ TL
//
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