LYS1_CANAL
ID LYS1_CANAL Reviewed; 382 AA.
AC P43065; A0A1D8PMA1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 {ECO:0000303|PubMed:7927784};
GN OrderedLocusNames=CAALFM_C405320WA {ECO:0000312|CGD:CAL0000179135};
GN ORFNames=orf19.1789.1;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=7927784; DOI=10.1128/iai.62.11.5027-5031.1994;
RA Garrad R.C., Schmidt T.M., Bhattacharjee J.K.;
RT "Molecular and functional analysis of the LYS1 gene of Candida albicans.";
RL Infect. Immun. 62:5027-5031(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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:0000305|PubMed:7927784}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P38998}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW29271.1; Type=Miscellaneous discrepancy; Note=The coordinates of this ORF in the reference genome reflect non-intron adjustments made to compensate for presumed sequencing errors.; Evidence={ECO:0000312|CGD:CAL0000179135};
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DR EMBL; U13233; AAA21362.1; -; Genomic_DNA.
DR EMBL; CP017626; AOW29271.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_443225.2; XM_443225.2.
DR AlphaFoldDB; P43065; -.
DR SMR; P43065; -.
DR STRING; 237561.P43065; -.
DR PRIDE; P43065; -.
DR GeneID; 6335429; -.
DR KEGG; cal:CAALFM_C405320WA; -.
DR CGD; CAL0000179135; LYS1.
DR eggNOG; KOG0172; Eukaryota.
DR OMA; YFFFSHT; -.
DR OrthoDB; 498994at2759; -.
DR UniPathway; UPA00033; UER00034.
DR Proteomes; UP000000559; Chromosome 4.
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..382
FT /note="Saccharopine dehydrogenase [NAD(+), L-lysine-
FT forming]"
FT /id="PRO_0000199010"
FT ACT_SITE 79
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT ACT_SITE 98
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 20
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 79
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 103
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 133
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 137
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 215..216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 291..293
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT BINDING 330..333
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P38998"
FT DISULFID 217..261
FT /evidence="ECO:0000250|UniProtKB:P38998"
SQ SEQUENCE 382 AA; 42394 MW; A3620191DF04B88F CRC64;
MSKSPVILHL RAETKPLEAR AALTPSTTKQ LLDAGFEIYV EESSQSTFDI KEYEAVGAKI
VPEGSWKTAP KERIIFGLKE LPENETFPLI HEHIQFAHCY KDQAGWQDVL KRFPQGNGIL
YDLEFLENDQ GRRVAAFGFY AGFAGAAIGV LDWSFKQLNG NTKGTKGEGE GGELPGVTPY
PNENELIKDV KIELEKALTK NGGQYPKCLV IGALGRCGSG AIDLFKKIGI PDDNIAKWDM
AETAKGGPFQ EIVDSDIFIN CIYLSKPIPP FINKEILNNE NRKLTTIVDV SADTTNPHNP
IPVYEIATVF NEPTVEVKLD KGPKLSVCSI DHLPSLLPRE ASEFFAKDLM PSLLELPNRD
TSPVWVRAKQ LFDKHVARLD KE
