LYS1_CANGA
ID LYS1_CANGA Reviewed; 372 AA.
AC Q6FU27;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=CAGL0F06875g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380952; CAG59191.1; -; Genomic_DNA.
DR RefSeq; XP_446267.1; XM_446267.1.
DR AlphaFoldDB; Q6FU27; -.
DR SMR; Q6FU27; -.
DR STRING; 5478.XP_446267.1; -.
DR EnsemblFungi; CAG59191; CAG59191; CAGL0F06875g.
DR GeneID; 2887663; -.
DR KEGG; cgr:CAGL0F06875g; -.
DR CGD; CAL0130944; CAGL0F06875g.
DR VEuPathDB; FungiDB:CAGL0F06875g; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_063085_0_0_1; -.
DR InParanoid; Q6FU27; -.
DR OMA; YFFFSHT; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; Peroxisome; Reference proteome.
FT CHAIN 1..372
FT /note="Saccharopine dehydrogenase [NAD(+), L-lysine-
FT forming]"
FT /id="PRO_0000199011"
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; 41552 MW; 9A578085727C3F2D CRC64;
MSVTLHLRGE TKPLEHRAAL TPTTVKHLIG KGFKIYVEES PQSIFKIDEY RRAGAIIVPF
GSWISAPRDR IIIGLKEMPE EDKFPLVHEH IQFAHCYKDQ AGWKDVLRRF INGNGTLYDL
EFLEDDNGRR VAAFGFYAGF AGAALGLADW AFKQTHKDSE DLPAVSPYPN EKALIKDIGK
AYKNALKTGA KKPKVLIIGA LGRCGSGAID FLKKVGLPEE NIIKWDIQET SRGGPFPEIA
ASDIFINCIY LSKPIAPFIN YELLNKPDRK LRTVVDVSAD TTNPHNPIPI YNIATVFNKP
TVKVNTSSGP KLSVISIDHL PSLLPREASE FFAHDLLPSL EQLPSRHVSP VWVRAEKLFN
RHSARAIRES KL
