ID A0A1I2GQ80_9BACT Unreviewed; 400 AA.
AC A0A1I2GQ80;
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=SAMN05216283_10359 {ECO:0000313|EMBL:SFF19190.1};
OS Sunxiuqinia elliptica.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=655355 {ECO:0000313|EMBL:SFF19190.1, ECO:0000313|Proteomes:UP000198964};
RN [1] {ECO:0000313|EMBL:SFF19190.1, ECO:0000313|Proteomes:UP000198964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFF19190.1,
RC ECO:0000313|Proteomes:UP000198964};
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; FONW01000003; SFF19190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2GQ80; -.
DR STRING; 655355.SAMN05216283_10359; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000198964; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF23; SACCHAROPINE DEHYDROGENASE [NAD(+), L-LYSINE-FORMING]; 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 Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|PIRSR:PIRSR018250-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198964};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..136
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 163..339
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 186..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ SEQUENCE 400 AA; 45584 MW; 165EA132E1743579 CRC64;
MKIGILRETR RWKDRRVAIT PETAAWIKQN YPTIDIVVQP SSLRVHKDEE YAQLGIPVVE
DISDCDLLIG VKEVANEALI EGKTYLMFAH VAKEQSHNQE FFRLMAQKKI TLIDYEYLVD
KHNDRLVAFG FWAGVVGAYY ALLGVAKRFC DMEIPGPEEC TDLNDLHRQL KAIPLPPLKF
LITGGGRVAS GALEIIKHLG IPEVLPHDFL LRDYDHPVFT RLDPEDYVER TDGQAYSNLH
FYEHPQLYHS SFLPYTKSAD VFIPCHFWNQ QSPDFFTKQD LLASDFSISL ISDISCDVPG
PIPTTLRTTE IEAPFYDVEP ESCSEKEAFS SKEHVTVVAV DNLPAALPFD ASRTFARDLY
YEVFPSLFGV DHHQIIERAT ILDKGKLTSC YSYLESFLND
//
