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Database: UniProt
Entry: A0A369QGW1_9BACT
LinkDB: A0A369QGW1_9BACT
Original site: A0A369QGW1_9BACT 
ID   A0A369QGW1_9BACT        Unreviewed;       446 AA.
AC   A0A369QGW1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Saccharopine dehydrogenase (NADP(+), L-lysine-forming) {ECO:0000313|EMBL:RDC63510.1};
DE            EC=1.5.1.8 {ECO:0000313|EMBL:RDC63510.1};
DE            EC=1.5.1.9 {ECO:0000313|EMBL:RDC63510.1};
GN   Name=aasS {ECO:0000313|EMBL:RDC63510.1};
GN   ORFNames=AHMF7616_02115 {ECO:0000313|EMBL:RDC63510.1};
OS   Adhaeribacter pallidiroseus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=2072847 {ECO:0000313|EMBL:RDC63510.1, ECO:0000313|Proteomes:UP000253919};
RN   [1] {ECO:0000313|EMBL:RDC63510.1, ECO:0000313|Proteomes:UP000253919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7616 {ECO:0000313|EMBL:RDC63510.1,
RC   ECO:0000313|Proteomes:UP000253919};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Adhaeribacter sp. HMF7616 genome sequencing and assembly.";
RL   Submitted (APR-2018) 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:RDC63510.1}.
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DR   EMBL; QASA01000001; RDC63510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369QGW1; -.
DR   OrthoDB; 973788at2; -.
DR   Proteomes; UP000253919; Unassembled WGS sequence.
DR   GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
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,
KW   ECO:0000313|EMBL:RDC63510.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253919}.
FT   DOMAIN          4..120
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          126..437
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   446 AA;  50418 MW;  49D5B3DB2729788A CRC64;
     MKHILLLGAG RSSVYLIDYL VAQAPSQNWH VTIADLQTAH LPARGLPSTF LSYLNLDIQE
     QAQLNSQVQK ADVVISLLPA IFHLPVAKAC LAIKRHFLTA SYVTPEIQAM HEAAKEHGLL
     FLMEMGLDPG IDHLSAKATI DRIREQGGQL FSFKSYTGGL VAPESDTNPW HYKISWNPRN
     VVLAGKGTAT YLYNHTPKYI PYSQLFRRTE QINVIDLGEL EGYANRDSLA YQKAYGLENI
     PTLIRGTLRW PGFCAAWHQL IKLGLTDDSY RLPDSENITY TQWLESYLPD NQLKKQDTID
     RLAHYLKLPG NSRELEAIRY LGLLESEKIK LKKATPAQIL EQRLVQRLAL QPTDQDLVVM
     QHEFEYGFNN QKKRLKSALV LTGQDATYTA MAQTVGMPLA FAAELLLTNE INLSGVHIPV
     LPELYRPLLA RLEKIGIQFT EQEENF
//
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