ID A0A1G8W8E0_9FLAO Unreviewed; 400 AA.
AC A0A1G8W8E0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN04487935_1692 {ECO:0000313|EMBL:SDJ74377.1};
OS Flavobacterium noncentrifugens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1128970 {ECO:0000313|EMBL:SDJ74377.1, ECO:0000313|Proteomes:UP000199580};
RN [1] {ECO:0000313|EMBL:SDJ74377.1, ECO:0000313|Proteomes:UP000199580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10076 {ECO:0000313|EMBL:SDJ74377.1,
RC ECO:0000313|Proteomes:UP000199580};
RA de Groot N.N.;
RL Submitted (OCT-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; FNEZ01000002; SDJ74377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8W8E0; -.
DR STRING; 1128970.SAMN04487935_1692; -.
DR OrthoDB; 1141481at2; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000199580; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199580}.
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 167..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"
SQ SEQUENCE 400 AA; 45371 MW; AD4C451198D5AAB1 CRC64;
MKFGIIKERK NPPDRRVVFT PEELQRLTKE HPEAQIKVES SDIRIFTDQQ YADLGIEIAT
DMTDCDVLFG VKEVPLEALI PNKKYFFFSH TIKKQPHNRK LLQAILDKKI DLYDHETIVD
AHFKRLIGFG RYAGIVGAYN GIRAFGIKFE LFNLPKAETL SGKDALVQKL KRQILPPIKI
VLTGHGKVGN GAKEILDAMK IKEVTVENYL TKVYSEPVYT QLDILDYNKR QDGKPSAKED
FYKNPTKYVS DFERFTKVSD IYMAGHFYAN DAPVILSLDM LRANDNKIKV VADISCDVDG
PIACTIKAST IAEPLFGFHP MENKEVDVFH PAAIVVMSVD NLPCELPKDA SEGFGEMFME
HVIPAFFNGD KDGILKRAKV TEDGHLTERF QYLKDYAKGK
//
