ID A0A2B7YR19_9EURO Unreviewed; 386 AA.
AC A0A2B7YR19;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=AJ80_02851 {ECO:0000313|EMBL:PGH23077.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH23077.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH23077.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH23077.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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}.
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:PGH23077.1}.
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DR EMBL; PDNA01000029; PGH23077.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7YR19; -.
DR STRING; 1447883.A0A2B7YR19; -.
DR OrthoDB; 5482984at2759; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000224634; 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; PF01262; AlaDh_PNT_C; 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:UP000224634}.
FT DOMAIN 7..147
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 195..327
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT BINDING 135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 215..216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 328..331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT DISULFID 217..259
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-4"
SQ SEQUENCE 386 AA; 42572 MW; F4F554E89E206327 CRC64;
MAPVTLHLRA EDKTLEHRSA LTPDTTRALI AAGYIVNVER SPTSPLRKRI FPDAQFEAAG
ATLVPEGSWV NVPSEHIILG LKELDETQNF PLKHAHVTFA HCYKNQGGWE RALGRWSRGN
GVLYDLEFLQ HDNGRRVAAF GYHAGFAGAA LALKNWAWQL EHPDGTPLPG VDGYTDGKGY
YANEEEMVNQ VREDVERAAK IAGRKPRVLV IGALGRCGRG AVDACVQAGC EDILRWDMAE
TAKGGPFTEI VESDIFINCI YLAEKIAPFV DRESLKSPSR KLSVVCDVSC DTTNPHNPIP
IYDINTTFDK PTVALEGVSN PPLSIISIDH LPSLLPAESS NAFSSDLLPF LLEIKNRDTN
PVWARAEKLF REKVQTLPTE LQKVEA
//
