(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 95.
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}.
DR   EMBL; AE016816; AAS51393.1; -; Genomic_DNA.
DR   RefSeq; NP_983569.1; NM_208922.1.
DR   SMR; Q75BV4; -.
DR   STRING; 33169.AAS51393; -.
DR   EnsemblFungi; AAS51393; AAS51393; AGOS_ACR167C.
DR   GeneID; 4619701; -.
DR   KEGG; ago:AGOS_ACR167C; -.
DR   HOGENOM; HOG000143704; -.
DR   InParanoid; Q75BV4; -.
DR   KO; K00290; -.
DR   OMA; YFFFSHT; -.
DR   UniPathway; UPA00033; UER00034.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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   PANTHER; PTHR11133:SF15; PTHR11133:SF15; 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; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BV4.
DR   SWISS-2DPAGE; Q75BV4.
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   NP_BIND         202..203
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   NP_BIND         317..320
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   REGION          278..280
FT                   /note="L-saccharopine binding"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
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                   /note="L-saccharopine"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         76
FT                   /note="L-saccharopine"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         100
FT                   /note="L-saccharopine"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         129
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         130
FT                   /note="L-saccharopine"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         134
FT                   /note="L-saccharopine; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         226
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         230
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         250
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P38998"
FT   BINDING         277
FT                   /note="NAD; via carbonyl oxygen"
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
//

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