ID A0A0X8HT17_9SACH Unreviewed; 372 AA.
AC A0A0X8HT17;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AW171_hschr42853 {ECO:0000313|EMBL:AMD20931.1};
OS Eremothecium sinecaudum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=45286 {ECO:0000313|EMBL:AMD20931.1, ECO:0000313|Proteomes:UP000243052};
RN [1] {ECO:0000313|EMBL:AMD20931.1, ECO:0000313|Proteomes:UP000243052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58844 {ECO:0000313|EMBL:AMD20931.1,
RC ECO:0000313|Proteomes:UP000243052};
RA Dietrich F.S.;
RT "Genome sequence of the yeast Holleya sinecauda.";
RL Submitted (JAN-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 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; CP014244; AMD20931.1; -; Genomic_DNA.
DR RefSeq; XP_017987927.1; XM_018132438.1.
DR AlphaFoldDB; A0A0X8HT17; -.
DR STRING; 45286.A0A0X8HT17; -.
DR GeneID; 28724200; -.
DR OrthoDB; 5482984at2759; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000243052; Chromosome iv.
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; 2.
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}.
FT DOMAIN 6..141
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 174..316
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-1"
FT BINDING 202..203
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"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
FT BINDING 317..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR018250-3"
SQ SEQUENCE 372 AA; 41584 MW; E5B1A82B53E63B0A CRC64;
MTVKLHLRAE TKPLEARAAL TPTSVRHLVK KGFKIYVEES PQSAFSSDEY KEAGAVLVPF
GSWKEAPLDR IIIGLKEMPE RDTFPLVHEH IQFAHCYKKQ AGWRDVLQRF VDGKGTLYDL
EFLEDDRGVR VAAFGFYAGF VGAALGLKDW AFKQTHSDSE EMDEVSPYDD EKKLVDDVRR
EYLEAIAAGA KEPTVLIIGA LGRCGRGARD FLRKCGIHEK NIKKWDMAET AVGGPFNEIA
EADIFINTIY LGKPIPPFIT MDLMDREDRK LSTIVDISAD TTSPHNPIPL YSVSTTFSKP
SLQVPTSIGP KLSVIAIDHL PSLLPREASE SFVSSLLPSL EQLGKRDTAP VWKRAKLLFD
KHCSLLDDRA KL
//
