ID A0A2I2GQA6_9EURO Unreviewed; 450 AA.
AC A0A2I2GQA6;
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=Lysine-ketoglutarate reductase/saccharopine dehydrogenase {ECO:0000313|EMBL:PLB55051.1};
GN ORFNames=P170DRAFT_432585 {ECO:0000313|EMBL:PLB55051.1};
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:PLB55051.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB55051.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB55051.1,
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 -!- 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:PLB55051.1}.
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DR EMBL; MSFO01000001; PLB55051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GQA6; -.
DR STRING; 1392250.A0A2I2GQA6; -.
DR VEuPathDB; FungiDB:P170DRAFT_432585; -.
DR OrthoDB; 2184985at2759; -.
DR Proteomes; UP000234275; 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:UP000234275}.
FT DOMAIN 10..124
FT /note="Saccharopine dehydrogenase NADP binding"
FT /evidence="ECO:0000259|Pfam:PF03435"
FT DOMAIN 128..443
FT /note="Saccharopine dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16653"
SQ SEQUENCE 450 AA; 49215 MW; CFA87C24693C8CA2 CRC64;
MPNQVAGSKV LLLGSGFVTK PTVEVLSKAD VNVTVACRTL ESAQKLSEGF KNTKAISLDV
NDPAALDKAL EQVDLVISLI PYTFHAVVIK SAIRTKKHVV TTSYVSPAMM ELDEECKKAG
ITVMNEIGLD PGIDHLYAVK TISEVHAEGG QITSFLSYCG GLPAPECSDN PLGYKFSWSS
RGVLLALRNA AKFYRDGKEF SVAGPDLMAT AKPYYIYPGF AFVAYPNRDS TPFRERYNIP
EAQDLVRGTL RYQGFPEMIK ALVDIDFLSD EPRETFNSPI AWKEATQQIL GAASSSEKDL
EAAISSKTAF ATSEDRNRII SGLRWIGIFS DEKITPRGNP LDTLCATLEK KMQYAPEERD
MVMLQHKFGI KHKDGSQETR TSTMCEYGVP GGYSAMAKTV GVPCGVAVKL VLDGTISEKG
VLAPMTMDIC APLLKTLKED YGIEMIEKTL
//
