LYS1_ASHGO
ID LYS1_ASHGO Reviewed; 372 AA.
AC Q75BV4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=LYS1; OrderedLocusNames=ACR167C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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:0000250|UniProtKB:P38998}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38998}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P38998}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
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DR EMBL; AE016816; AAS51393.1; -; Genomic_DNA.
DR RefSeq; NP_983569.1; NM_208922.1.
DR AlphaFoldDB; Q75BV4; -.
DR SMR; Q75BV4; -.
DR STRING; 33169.AAS51393; -.
DR EnsemblFungi; AAS51393; AAS51393; AGOS_ACR167C.
DR GeneID; 4619701; -.
DR KEGG; ago:AGOS_ACR167C; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_063085_0_0_1; -.
DR InParanoid; Q75BV4; -.
DR OMA; YFFFSHT; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; Peroxisome; Reference proteome.
FT CHAIN 1..372
FT /note="Saccharopine dehydrogenase [NAD(+), L-lysine-
FT forming]"
FT /id="PRO_0000199009"
FT MOTIF 370..372
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 76
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 17
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 76
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 202..203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 278..280
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 317..320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT DISULFID 204..248
FT /evidence="ECO:0000250|UniProtKB:P38998"
SQ SEQUENCE 372 AA; 40974 MW; 6A6B7154788F1799 CRC64;
MSAILHLRAE TKPMEARAAL TPTTVRTLVS HGFKIYVEES AQSVFEAAEY AAAGAEVVAT
GSWRGAPRER IIVGLKELPE EDTFPLEHTH IQFAHCYKNQ SGWREVLGRF QSGGGLLYDL
EFLQDDRGRR VAAFGYYAGF AGAALGLRDW AWKQTHTDAE DLPAVAPYEN EQALVSEVAA
ACEEAYKKGA RKPRVLVIGA LGRCGSGAVE LLRQCGLHDK HIIRWDIAET ARGGPFPEIA
AADIFINCIY LSQPIAPFIN MELLDRPDRK LRTIVDVSAD TTNPHNPVPV YNVATVFSSP
TVVVPTSQGP KLSVISIDHL PSLLPREASE AFASDLLPSL LQLPERDTAP VWLRAKELFQ
QHCERLSKEA RL
