ID A0A0X7BFS4_9FLAO Unreviewed; 398 AA.
AC A0A0X7BFS4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AP058_00427 {ECO:0000313|EMBL:KVV15992.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV15992.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV15992.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV15992.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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}.
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:KVV15992.1}.
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DR EMBL; LLWK01000028; KVV15992.1; -; Genomic_DNA.
DR RefSeq; WP_066306366.1; NZ_LLWK01000028.1.
DR AlphaFoldDB; A0A0X7BFS4; -.
DR STRING; 1729581.AP058_00427; -.
DR PATRIC; fig|1729581.3.peg.456; -.
DR OrthoDB; 1141481at2; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000059935; 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; PF01262; AlaDh_PNT_C; 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:UP000059935}.
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 157..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 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ SEQUENCE 398 AA; 44877 MW; 7E6284E9B730E50E CRC64;
MKFGIIKERK NPPDRRVVFA PDELAKIKQQ FTTAQFVVES SDIRIFPDVA YTNMGVSVTD
DLSDCDVLIG VKEVPITNLI PNKSYFFFSH TIKKQPYNRD LLRSILEKNI TLYDHETIVD
ANNRRLIGFG RYAGMVGIYN GIRAFGLKFE LFKLPKAETL DGREGLLKQL KRITLPPIKF
VVTGTGKVGG GVKEILDAIK VKEVSKENYL TKKYAQPVYV QLDVLDYNVR KDGKQLAYTD
FYKNPTEYES SFDTFTKVSD IFVAAHFYAA EAPIILTREM LQAIDCNIRV IADISCDING
PIAATLRSST IAEPLYGYLA SENKEVDVFH PAAIVVMAVD NLPCEIPKDA SFGFGEQFLE
HVLPAFFNND KDGILARAKV TENGKLTKRF EYLQDFIS
//
