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UniProtKB/Swiss-Prot entry P38999


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

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Entry information
Entry name LYS9_YEAST
Primary accession number P38999
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    July 22, 2008 (Entry version 72)
Name and origin of the protein
Protein name Saccharopine dehydrogenase [NADP+, L-glutamate-forming]
Synonyms EC 1.5.1.10
Saccharopine reductase
Gene name
Name: LYS9
Synonyms: LYS13
OrderedLocusNames: YNR050C
ORFNames: N3461
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1278B;
Feller A.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873 [NCBI, ExPASy, EBI, Israel, Japan]
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.";
Nature 387:93-98(1997).
[3]
PROTEIN SEQUENCE OF 314-324.
STRAIN=ATCC 38531 / Y41;
DOI=10.1016/0378-1097(96)00006-7; PubMed=8935650 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
INTERACTION WITH TRM112.
DOI=10.1128/MCB.25.11.4359-4370.2005; PubMed=15899842 [NCBI, ExPASy, EBI, Israel, Japan]
Purushothaman S.K., Bujnicki J.M., Grosjean H., Lapeyre B.;
"Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA.";
Mol. Cell. Biol. 25:4359-4370(2005).
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
X77363; CAA54552.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71665; CAA96331.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S41937; S41937.
RefSeq NP_014448.1; -.
3D structure databases
PDB
2AXQ; X-ray; 1.70 A; A=1-446.[ExPASy / RCSB / EBI]
PDBsum 2AXQ; -.
ModBase P38999.
Protein-protein interaction databases
DIP DIP:776N; -.
IntAct P38999; -.
Organism-specific databases
CYGD YNR050c; -.
SGD S000005333; LYS9.
Yeast-GFP YNR050C.
Gene expression databases
ArrayExpress P38999; -.
GermOnline YNR050C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004755; Molecular function: saccharopine dehydrogenase (NADP+, L-glutamate-forming) activity (traceable author statement from SGD).
GO:0019878; Biological process: lysine biosynthetic process via aminoadipic acid (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR005097; Saccharopine_DHase.
Graphical view of domain structure.
Pfam PF03435; Saccharop_dh; 1.
Pfam graphical view of domain structure.
BLOCKS P38999.
Proteomic databases
PeptideAtlas P38999; -.
Genome annotation databases
Ensembl YNR050C; Saccharomyces cerevisiae. [Contig view]
GeneID 855786; -.
GenomeReviews Y13139_GR; YNR050C.
KEGG sce:YNR050C; -.
NMPDR fig|4932.3.peg.5529; -.
Phylogenomic databases
HOGENOM P38999; -.
Other
LinkHub P38999; -.
ProtoNet P38999.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; Lysine biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   446  446     Saccharopine dehydrogenase [NADP+, L-glutamate-forming]. PRO_0000212839
STRAND   3     8  6      
HELIX   14    22  9      
STRAND   27    35  9      
HELIX   36    43  8      
TURN   44    47  4      
STRAND   49    52  4      
HELIX   58    66  9      
STRAND   68    73  6      
HELIX   77    79  3      
HELIX   80    90  11      
STRAND   93    96  4      
HELIX   102   114  13      
STRAND   117   119  3      
TURN   124   126  3      
HELIX   128   142  15      
STRAND   146   158  13      
HELIX   160   162  3      
STRAND   171   173  3      
HELIX   176   180  5      
HELIX   181   183  3      
STRAND   186   190  5      
STRAND   193   197  5      
TURN   199   201  3      
HELIX   202   205  4      
STRAND   217   221  5      
HELIX   228   231  4      
STRAND   238   247  10      
HELIX   250   259  10      
TURN   260   263  4      
HELIX   269   271  3      
HELIX   277   285  9      
STRAND   288   291  4      
HELIX   292   300  9      
HELIX   308   320  13      
TURN   321   324  4      
HELIX   335   346  12      
STRAND   355   366  12      
STRAND   372   382  11      
HELIX   390   407  18      
STRAND   414   417  4      
HELIX   422   436  15      
STRAND   441   444  4      
Sequence information
Length: 446 AA [This is the length of the unprocessed precursor] Molecular weight: 48918 Da [This is the MW of the unprocessed precursor] CRC64: 1EC4CE1CE3BCD916 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGKNVLLLGS GFVAQPVIDT LAANDDINVT VACRTLANAQ ALAKPSGSKA ISLDVTDDSA 

        70         80         90        100        110        120 
LDKVLADNDV VISLIPYTFH PNVVKSAIRT KTDVVTSSYI SPALRELEPE IVKAGITVMN 

       130        140        150        160        170        180 
EIGLDPGIDH LYAVKTIDEV HRAGGKLKSF LSYCGGLPAP EDSDNPLGYK FSWSSRGVLL 

       190        200        210        220        230        240 
ALRNSAKYWK DGKIETVSSE DLMATAKPYF IYPGYAFVCY PNRDSTLFKD LYHIPEAETV 

       250        260        270        280        290        300 
IRGTLRYQGF PEFVKALVDM GMLKDDANEI FSKPIAWNEA LKQYLGAKST SKEDLIASID 

       310        320        330        340        350        360 
SKATWKDDED RERILSGFAW LGLFSDAKIT PRGNALDTLC ARLEELMQYE DNERDMVVLQ 

       370        380        390        400        410        420 
HKFGIEWADG TTETRTSTLV DYGKVGGYSS MAATVGYPVA IATKFVLDGT IKGPGLLAPY 

       430        440 
SPEINDPIMK ELKDKYGIYL KEKTVA 

P38999 in FASTA format

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