ID A0A1Y2X4J5_9PEZI Unreviewed; 447 AA.
AC A0A1Y2X4J5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Saccharopine dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=K445DRAFT_10407 {ECO:0000313|EMBL:OTB16855.1};
OS Daldinia sp. EC12.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB16855.1, ECO:0000313|Proteomes:UP000243732};
RN [1] {ECO:0000313|EMBL:OTB16855.1, ECO:0000313|Proteomes:UP000243732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC12 {ECO:0000313|EMBL:OTB16855.1,
RC ECO:0000313|Proteomes:UP000243732};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR EMBL; KZ112934; OTB16855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2X4J5; -.
DR STRING; 1001832.A0A1Y2X4J5; -.
DR OrthoDB; 2184985at2759; -.
DR Proteomes; UP000243732; 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:UP000243732}.
FT DOMAIN 6..120
FT /note="Saccharopine dehydrogenase NADP binding"
FT /evidence="ECO:0000259|Pfam:PF03435"
FT DOMAIN 124..439
FT /note="Saccharopine dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16653"
SQ SEQUENCE 447 AA; 49308 MW; 41D5F5CD11E094E5 CRC64;
MSSQKVLMLG AGFVTLPTLH ILSDAGIAVT VACRTLASAQ SLAKGVKHAT PISLDVNDDK
ALDAEVGKHD LVISLIPYTF HATVIKSAIR QKKHVVTTSY VSPAMLELDQ QAKDAGITVM
NEIGLDPGID HLYAVKTIEE VHKAGGKILT FLSYCGGLPA PENSDNPLGY KFSWSSRGVL
LALRNAAKYW QDGKVVEVAS KDLMATAKPY FIYPGYAFVA YPNRDSTPYK ERYNIPEAQT
IIRGTLRYQG FPEFIRVLVD IGFLDDTEQD FLKQPITWKE ATQKILGASA SSQGDLESTI
ASKARFDSPE EKTRILSGLR WIGIFSDEKI TPRGNPLDTL CATLEKKMQY EEGERDFVML
QHKFEIENKD GSREVRTSTL CEYGDPKGYS AMAKLVGVPC GVAVKQVLDG TISERGILAP
MNSKINDPLM KELKEKYGIF LKEKTIL
//
