LYS1_NEUCR
ID LYS1_NEUCR Reviewed; 372 AA.
AC Q7SFX6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming];
DE Short=SDH;
DE EC=1.5.1.7;
DE AltName: Full=Lysine--2-oxoglutarate reductase;
GN Name=lys-4; ORFNames=NCU03118;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=14304863;
RA Trupin J.S., Broquist H.P.;
RT "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine
RT biosynthesis. I. Studies in Neurospora crassa.";
RL J. Biol. Chem. 240:2524-2530(1965).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-
CC lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate
CC (AAA) pathway for lysin biosynthesis. {ECO:0000250|UniProtKB:P38998}.
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:0000250|UniProtKB:P38998};
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:0000305|PubMed:14304863}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38998}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; CM002236; EAA35741.1; -; Genomic_DNA.
DR RefSeq; XP_964977.1; XM_959884.3.
DR AlphaFoldDB; Q7SFX6; -.
DR SMR; Q7SFX6; -.
DR STRING; 5141.EFNCRP00000002800; -.
DR EnsemblFungi; EAA35741; EAA35741; NCU03118.
DR GeneID; 3881135; -.
DR KEGG; ncr:NCU03118; -.
DR VEuPathDB; FungiDB:NCU03118; -.
DR HOGENOM; CLU_063085_0_0_1; -.
DR InParanoid; Q7SFX6; -.
DR OMA; YFFFSHT; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
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 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 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; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Disulfide bond; Lysine biosynthesis; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..372
FT /note="Saccharopine dehydrogenase [NAD(+), L-lysine-
FT forming]"
FT /id="PRO_0000199013"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 18
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 77
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 100
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 129
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 130
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 134
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 200..201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 224
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 276..278
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 316..319
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT DISULFID 202..246
FT /evidence="ECO:0000250|UniProtKB:P38998"
SQ SEQUENCE 372 AA; 40877 MW; 7300490C46C40592 CRC64;
MAPTVLHLRS ETKHLEHRSA LTPTTTAELI KAGYIVNVER SPERIFDDEE FEKAGATLVP
EHSWVDAPKE HIIVGLKELE EKDFPLKHVH VQFAHCYKQQ AGWENVLARF PRGGGTLLDL
EFLVDEHGRR VAAFGFHAGF AGAALALEVW AWQLNHSEPF PGVESYPNED ALIADVKKAV
KEGVEAAGRL PRVIVIGARG RCGSGAVSAL KKAGIPDENI LDWDMAETAK GGPFKEITDS
DIFVNCIYLT SKIPNFVNME SLQVPDRQLR VVCDVSADTT SPFTPVPIYT VATTFDKPTV
PVDGLTSGPP LSVISIDHLP SLLPREASEA FSHDLLPSLL TLNDWQNSPV WARAKQLFDE
KVATLPESAL QK
