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Database: UniProt
Entry: A0A1M3HNU9_9SPHI
LinkDB: A0A1M3HNU9_9SPHI
Original site: A0A1M3HNU9_9SPHI 
ID   A0A1M3HNU9_9SPHI        Unreviewed;       430 AA.
AC   A0A1M3HNU9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Saccharopine dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGO55_17185 {ECO:0000313|EMBL:OJW60202.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW60202.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW60202.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW60202.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJW60202.1}.
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DR   EMBL; MKTZ01000002; OJW60202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3HNU9; -.
DR   STRING; 1895841.BGO55_17185; -.
DR   Proteomes; UP000184242; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; SACCHAROPINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          5..121
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          127..423
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   430 AA;  47816 MW;  8518A7AC31134DC7 CRC64;
     MNKHILLFGA GKSATCLIQF LDRTVSSRDW QLTVAESNLE LAQSKLSGSP HTKAVQVSVE
     DREQRDNLIR QADIVISLLP PALHFLVATS CIEWKKHLLT ASYLDDKLRA LEPAIRDKGL
     LFLCEMGLDP GIDHMSAMQL IHRIREQGGQ VHSFLSHTGG LVSPVSDDNP WHYKISWNPR
     NVVLAGSAGA KYLENGQTVT RTYEELFRRI NKVEIKELAS LAWYPNRDSL SYIPVYGLDG
     INTFIRTTLR YPDYIRAWSA IVDAHLTDDK TPLSLSKDNV TIAQWSSPIR PLVDDSIRSQ
     LEYLGLFSDE PIPPSAHTSA DVLQYLLETR LAMRPGDRDM IVMLHEIAYT TAASPGVTRR
     ITSSLVVHGE DHLRTAMAKT VGLPLGIAAV SILEGKIKLT GLHIPISPGI YTPVMEELAL
     QGIRFVEEGS
//
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