ID A0A0B7FII2_THACB Unreviewed; 368 AA.
AC A0A0B7FII2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming] {ECO:0000256|ARBA:ARBA00021221, ECO:0000256|PIRNR:PIRNR018250};
DE Short=SDH {ECO:0000256|PIRNR:PIRNR018250};
DE EC=1.5.1.7 {ECO:0000256|ARBA:ARBA00012847, ECO:0000256|PIRNR:PIRNR018250};
DE AltName: Full=Lysine--2-oxoglutarate reductase {ECO:0000256|ARBA:ARBA00033228, ECO:0000256|PIRNR:PIRNR018250};
GN Name=LYS1 {ECO:0000313|EMBL:CEL56739.1};
GN ORFNames=RSOLAG1IB_08041 {ECO:0000313|EMBL:CEL56739.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL56739.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL56739.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL56739.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) 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 ECO:0000256|PIRNR:PIRNR018250};
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, ECO:0000256|PIRNR:PIRNR018250}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|PIRNR:PIRNR018250}.
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DR EMBL; LN679124; CEL56739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7FII2; -.
DR STRING; 1108050.A0A0B7FII2; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000059188; 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; cd12188; SDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR027281; Lys1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR018250};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW ECO:0000256|PIRNR:PIRNR018250};
KW NAD {ECO:0000256|PIRNR:PIRNR018250, ECO:0000256|PIRSR:PIRSR018250-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR018250};
KW Reference proteome {ECO:0000313|Proteomes:UP000059188}.
FT DOMAIN 8..142
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 172..311
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 194..195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 242
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 312..315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT DISULFID 196..240
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-4"
SQ SEQUENCE 368 AA; 40318 MW; A885BD6BEB10F114 CRC64;
MSSRPTFWLR CEKKEFERRA ALTPTTAKKL IDAGFDITVE RDPQRIFDDE EYETVGCTLA
EHNSWPSAPV TTPIIGLKEL PVSTDPLPHT HIQFAHCYKR QGGWADVLAR FYHGGGTLYD
LEFLTDASGR RVAAFGYHAG FAGAAAGCLA YAAQAEGGNL GELVPYENEG KMVDAVKGVI
GGRKLRALVI GALGRCGRGA VDLFRKVGLE EDDIVKWDMA ETAKGGPFQE ILDVDIFVNC
IYLSSKIPSF LTHEQINAAG KDRRLSVVVD VSCDTTNPNN PIPIYNINTT FDKPTVPVKV
GAGNPPMTVI SIDHLPTLLP REASEQFSSD LLPSLLEFPN RKEARVWTEA EALFKAKLAE
AKAELNLQ
//
