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UniProtKB/Swiss-Prot entry P38997


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LYS1_YARLI
Primary accession number P38997
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 55)
Name and origin of the protein
Protein name Saccharopine dehydrogenase [NAD+, L-lysine-forming]
Synonyms SDH
EC 1.5.1.7
Lysine--2-oxoglutarate reductase
Gene name
Name: LYS5
OrderedLocusNames: YALI0B15444g
From
Yarrowia lipolytica (Candida lipolytica) [TaxID: 4952] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
PubMed=2388625 [NCBI, ExPASy, EBI, Israel, Japan]
Xuan J.-W., Fournier P., Declerck N., Chasles M., Gaillardin C.;
"Overlapping reading frames at the LYS5 locus in the yeast Yarrowia lipolytica.";
Mol. Cell. Biol. 10:4795-4806(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CLIB 122 / E 150;
DOI=10.1038/nature02579; PubMed=15229592 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M34929; AAA35248.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR382128; CAG83182.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A36467; A36467.
RefSeq XP_500931.1; -.
3D structure databases
ModBase P38997.
Ontologies
GO
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0004754; Molecular function: saccharopine dehydrogenase (NAD+, L-lysine-forming) activity (inferred from electronic annotation from EC).
GO:0009085; Biological process: lysine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR007698; Ala_DHase/PNT_C.
IPR007886; Ala_DHase/PNT_N.
Graphical view of domain structure.
Pfam PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.
ProtoNet P38997.
Genome annotation databases
GeneID 2907616; -.
KEGG yli:YALI0B15444g; -.
Phylogenomic databases
HOGENOM P38997; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   369  369     Saccharopine dehydrogenase [NAD+, L-lysine-forming]. PRO_0000199015
ACT_SITE   205   205        By similarity. 
Sequence information
Length: 369 AA [This is the length of the unprocessed precursor] Molecular weight: 40612 Da [This is the MW of the unprocessed precursor] CRC64: B1B749FA008B8A36 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTAPVKLHLR AETKPLEHRS ALTPTTTRKL LDAGFEVFVE KSPLRIFDDQ EFVDVGATLV 

        70         80         90        100        110        120 
EEGSWVSAPE DRMIIGLKEL PEESFPLSHE HIQFAHCYKD QGGWKDVLSR FPAGNGTLYD 

       130        140        150        160        170        180 
LEFLEDDNGR RVAAFGFHAG FAGAAIGVET WAFQQTHPDS ENLPGVSAYP NETELVDKIK 

       190        200        210        220        230        240 
KDLAAAVEKG SKLPTVLVIG ALGRCGSGAI DLARKVGIPE ENIIRWDMNE TKKGGPFQEI 

       250        260        270        280        290        300 
ADADIFINCI YLSQPIPPFI NYDLLNKETR KLSVIVDVSA DTTNPHNPVP VYTIATTFDH 

       310        320        330        340        350        360 
PTVPVETTAG PKLSVCSIDH LPSLLPREAS EAFSEALLPS LLQLPQRDTA PVWTRAKALF 


DKHVLRIGE 

P38997 in FASTA format

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