ID A0A3N4HNU7_ASCIM Unreviewed; 448 AA.
AC A0A3N4HNU7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=Apo Saccharopine reductase {ECO:0000313|EMBL:RPA75495.1};
GN ORFNames=BJ508DRAFT_418072 {ECO:0000313|EMBL:RPA75495.1};
OS Ascobolus immersus RN42.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascobolaceae; Ascobolus.
OX NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA75495.1, ECO:0000313|Proteomes:UP000275078};
RN [1] {ECO:0000313|EMBL:RPA75495.1, ECO:0000313|Proteomes:UP000275078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN42 {ECO:0000313|EMBL:RPA75495.1,
RC ECO:0000313|Proteomes:UP000275078};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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DR EMBL; ML119762; RPA75495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4HNU7; -.
DR STRING; 1160509.A0A3N4HNU7; -.
DR Proteomes; UP000275078; 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:UP000275078}.
FT DOMAIN 5..119
FT /note="Saccharopine dehydrogenase NADP binding"
FT /evidence="ECO:0000259|Pfam:PF03435"
FT DOMAIN 123..437
FT /note="Saccharopine dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16653"
SQ SEQUENCE 448 AA; 48706 MW; 98A3D7D808D34644 CRC64;
MAPSVLLLGS GFVAKPCLDV LADAGINVTV ACRTLSTAQS LAGTTKNTSA ISLDVNDAAA
LEAETAKHDL VISLIPYTYH AQVIKAAIAA KKHVVTTSYV SPAMMELDAA AKEAGITVMN
EIGLDPGIDH LYAVKTIDEV HAAGGKIISF LSYCGGLPAP EDSGNPLGYK FSWSSRGVLL
ALRNSAKYWE NGKVVEVEGP ELMATAKPYF IYPGYAFICY PNRDSTPYKE RYNIPEAQTI
IRGTLRYQGF AEFIKVLVDV GFLSEEQKDF LQKGSDLTWK QALAKILGVE STDENDLVAA
ISSKTKFPSE DEKKRILSGF KWLGLFSDDK ITPRGTPLDT LCATLEQKMQ YEEGERDLVM
LQHKFEIENA DGSRETRTST MVEYGDPKGY SAMAKTVGVP CAVAVQAVLN GTISDKGVLA
PMNAKINNPL MKELKEKYNI ECIEKVVS
//
