ID   A0A1M5KBM3_9FLAO        Unreviewed;       402 AA.
AC   A0A1M5KBM3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming] {ECO:0000256|ARBA:ARBA00021221};
DE            EC=1.5.1.7 {ECO:0000256|ARBA:ARBA00012847};
DE   AltName: Full=Lysine--2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00033228};
GN   ORFNames=SAMN05444148_0284 {ECO:0000313|EMBL:SHG50182.1};
OS   Winogradskyella jejuensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1089305 {ECO:0000313|EMBL:SHG50182.1, ECO:0000313|Proteomes:UP000184522};
RN   [1] {ECO:0000313|EMBL:SHG50182.1, ECO:0000313|Proteomes:UP000184522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25330 {ECO:0000313|EMBL:SHG50182.1,
RC   ECO:0000313|Proteomes:UP000184522};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-
CC         lysine + NADH; Xref=Rhea:RHEA:12440, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57951; EC=1.5.1.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001177};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004884}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR   EMBL; FQWS01000001; SHG50182.1; -; Genomic_DNA.
DR   RefSeq; WP_073082012.1; NZ_FQWS01000001.1.
DR   AlphaFoldDB; A0A1M5KBM3; -.
DR   STRING; 1089305.SAMN05444148_0284; -.
DR   OrthoDB; 1141481at2; -.
DR   UniPathway; UPA00033; UER00034.
DR   Proteomes; UP000184522; Unassembled WGS sequence.
DR   GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd05199; SDH_like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR027281; Lys1.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11133:SF22; SACCHAROPINE DEHYDROGENASE [NADP(+), L-GLUTAMATE-FORMING]-RELATED; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF018250; Saccharopine_DH_Lys; 2.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   NAD {ECO:0000256|PIRSR:PIRSR018250-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          4..136
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          165..338
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
FT   ACT_SITE        72
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   ACT_SITE        90
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT   BINDING         223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT   BINDING         294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ   SEQUENCE   402 AA;  45125 MW;  71E9482F75B049D6 CRC64;
     MKFAIIKERK NPPDRRVVFS PEKLAEARAQ FPNAEFMVES SDIRIFPDIA YADLGFKVTD
     DVSDADVMIG VKEVPIDHLI PNKKYFYFSH TIKKQPYNRK LLQAMLDKGI EMYDHETIVK
     RSGARLIGFG RYAGLVGAYN GFRALGLRDG LFNLPKVESL SDLDAVKAEL DKIILPNIKI
     LLTGTGKVAY GAKEILDHLG IKQVSDALYL TSEFTEPVYC MADVMEYAKR KDGKVGEKYA
     FYKDPSGYES NFMPYAKQTD YFIAGHFYGD GAPYLFTRQD AKHPDFRINL VADVSCDIDG
     PVASTIRPST IADPFYGYNP QTEAEVAFNA NDAITVMAVD NLPCELPKDA SEGFGDAFLE
     HVIPAFFNDD KDGILQRAKM TTSDGKLTKR YNYLQDYVDG KE
//