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
//