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UniProtKB/Swiss-Prot entry P43065


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

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Entry information
Entry name LYS1_CANAL
Primary accession number P43065
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
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: LYS1
From
Candida albicans (Yeast) [TaxID: 5476] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7927784 [NCBI, ExPASy, EBI, Israel, Japan]
Garrad R.C., Schmidt T.M., Bhattacharjee J.K.;
"Molecular and functional analysis of the LYS1 gene of Candida albicans.";
Infect. Immun. 62:5027-5031(1994).
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
U13233; AAA21362.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase P43065.
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 P43065.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Lysine biosynthesis; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   382  382     Saccharopine dehydrogenase [NAD+, L-lysine-forming]. PRO_0000199010
ACT_SITE   217   217        By similarity. 
Sequence information
Length: 382 AA [This is the length of the unprocessed precursor] Molecular weight: 42394 Da [This is the MW of the unprocessed precursor] CRC64: A3620191DF04B88F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKSPVILHL RAETKPLEAR AALTPSTTKQ LLDAGFEIYV EESSQSTFDI KEYEAVGAKI 

        70         80         90        100        110        120 
VPEGSWKTAP KERIIFGLKE LPENETFPLI HEHIQFAHCY KDQAGWQDVL KRFPQGNGIL 

       130        140        150        160        170        180 
YDLEFLENDQ GRRVAAFGFY AGFAGAAIGV LDWSFKQLNG NTKGTKGEGE GGELPGVTPY 

       190        200        210        220        230        240 
PNENELIKDV KIELEKALTK NGGQYPKCLV IGALGRCGSG AIDLFKKIGI PDDNIAKWDM 

       250        260        270        280        290        300 
AETAKGGPFQ EIVDSDIFIN CIYLSKPIPP FINKEILNNE NRKLTTIVDV SADTTNPHNP 

       310        320        330        340        350        360 
IPVYEIATVF NEPTVEVKLD KGPKLSVCSI DHLPSLLPRE ASEFFAKDLM PSLLELPNRD 

       370        380 
TSPVWVRAKQ LFDKHVARLD KE 

P43065 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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