ID B0Y6W5_ASPFC Unreviewed; 450 AA.
AC B0Y6W5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:EDP50500.1};
GN ORFNames=AFUB_068370 {ECO:0000313|EMBL:EDP50500.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP50500.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP50500.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS499598; EDP50500.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y6W5; -.
DR SMR; B0Y6W5; -.
DR EnsemblFungi; EDP50500; EDP50500; AFUB_068370.
DR VEuPathDB; FungiDB:AFUB_068370; -.
DR HOGENOM; CLU_016207_3_1_1; -.
DR PhylomeDB; B0Y6W5; -.
DR Proteomes; UP000001699; 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}.
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; 49450 MW; 4CAC6FFC43FB85DA CRC64;
MVKQIAGSKV LLLGSGFVTK PTVEVLTKAD VHVTVACRTL ESAQKLCQGF PNTKAIALDV
NDAAALDKAL EQADLAISLI PYTFHALVIK SAIRTKKHVV TTSYVSPAMM ELDEECKKAG
ITVMNEIGLD PGIDHLYAVK TISEVHAEGG KITSFLSYCG GLPAPECSDN PLGYKFSWSS
RGVLLALRNA AKFYQDGKEF SVAGPDLMAT AKPYYIYPGY AFVAYPNRDS CPYRERYQIP
EAQTVIRGTL RYQGFPEMIK VLVDIGFLSD EAKDFLNSPI PWKEATQKIL GATSSDEKDL
EWAIASKTTF TDNDSRNRLI SGLRWIGLFS DEQITPRGNP LDTLCATLER KMQYGPGERD
MVMLQHKFGI EHKDGSKETR TSTLVEYGDP NGYSAMAKTV GVPCGVAVKL VLDGTISQKG
VLAPMTWDIC EPLLKTLKEE YGIEMIEKTV
//
