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Database: UniProt
Entry: A0A1Y2BZ43_9FUNG
LinkDB: A0A1Y2BZ43_9FUNG
Original site: A0A1Y2BZ43_9FUNG 
ID   A0A1Y2BZ43_9FUNG        Unreviewed;       448 AA.
AC   A0A1Y2BZ43;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:ORY40038.1};
GN   ORFNames=LY90DRAFT_458712 {ECO:0000313|EMBL:ORY40038.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY40038.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY40038.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY40038.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-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:ORY40038.1}.
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DR   EMBL; MCOG01000129; ORY40038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2BZ43; -.
DR   STRING; 1754190.A0A1Y2BZ43; -.
DR   OrthoDB; 2184985at2759; -.
DR   Proteomes; UP000193920; 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:UP000193920}.
FT   DOMAIN          7..122
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          126..441
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   448 AA;  49129 MW;  F1390293BE82C9DD CRC64;
     MVAEKKILLI GSGFVAGPCL NYLLRRPENK ITVACRTISK AQALCNGHAN ATPITLDVSN
     EAQLDAEVAK HDIVINLIPY IYHPIVIKSC IKNKKHCCTT SYVSPVMAEM DEAAKAADVT
     CMNEIGIDPG VDHLYALKVI NEVHERKGKI ISFTSWCGGL PVPEDSNNPL GYKFSWSARG
     VLLALRNNAR YLKDGKIVEI ENVNGALMKS AKPVIIYPGY AFVGYPNRDS LSYLERYHIP
     EAKNCMRGTL RYQGFPEFAQ ALAEVGFLDD SPKDFLSSPI PWNAALAKLL GIEATDAASL
     KQAVTEKCHL EGENKNSILY GFNWLGLFSD TPIVPNGNAL DCLCATLEQK LQYGPNERDL
     CVLQHKFEIE EADGSITNVN STGFWTGVVG GDSAMATTVG LPCGIAVQLI LDGVIKRRGV
     IAPMEKDVYE PIRETLAKEG VYMVEEKW
//
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