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UniProtKB/Swiss-Prot entry P07702


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

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Entry information
Entry name LYS2_YEAST
Primary accession number P07702
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on March 1, 1992 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 96)
Name and origin of the protein
Protein name L-aminoadipate-semialdehyde dehydrogenase
Synonyms EC 1.2.1.31
Alpha-aminoadipate reductase
Alpha-AR
Gene name
Name: LYS2
OrderedLocusNames: YBR115C
ORFNames: YBR0910
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].
DOI=10.1016/0378-1119(91)90117-T; PubMed=2013406 [NCBI, ExPASy, EBI, Israel, Japan]
Morris M.E., Jinks-Robertson S.;
"Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae: homology to Bacillus brevis tyrocidine synthetase 1.";
Gene 98:141-145(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/yea.320101014; PubMed=7900426 [NCBI, ExPASy, EBI, Israel, Japan]
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
"Analysis of a 70 kb region on the right arm of yeast chromosome II.";
Yeast 10:1363-1381(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 1209-1392.
DOI=10.1016/0378-1119(86)90408-7; PubMed=3542721 [NCBI, ExPASy, EBI, Israel, Japan]
Fleig U.N., Pridmore R.D., Philippsen P.;
"Construction of LYS2 cartridges for use in genetic manipulations of Saccharomyces cerevisiae.";
Gene 46:237-245(1986).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1083-1392.
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/yea.320080507; PubMed=1626431 [NCBI, ExPASy, EBI, Israel, Japan]
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
"Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins.";
Yeast 8:397-408(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
STRAIN=ATCC 204508 / S288c;
PubMed=7916691 [NCBI, ExPASy, EBI, Israel, Japan]
Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K., Feldmann H.;
"TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning, sequence and deletion analysis of the gene.";
Eur. J. Biochem. 217:487-492(1993).
[7]
PHOSPHOPANTETHEINYLATION AT SER-880, AND MASS SPECTROMETRY.
DOI=10.1021/bi9829940; PubMed=10320345 [NCBI, ExPASy, EBI, Israel, Japan]
Ehmann D.E., Gehring A.M., Walsh C.T.;
"Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5.";
Biochemistry 38:6171-6177(1999).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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
M36287; AAA34747.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X66247; CAA46975.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X78993; CAA55617.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35984; CAA85072.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X73532; CAA51938.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JU0448; YGBYAD.
RefSeq NP_009673.1; -.
3D structure databases
HSSP O30409; 1DNY. [HSSP ENTRY / PDB]
ModBase P07702.
Protein-protein interaction databases
DIP DIP:6811N; -.
IntAct P07702; 7.
Organism-specific databases
CYGD YBR115c; -.
SGD S000000319; LYS2.
Yeast-GFP YBR115C.
Gene expression databases
ArrayExpress P07702; -.
GermOnline YBR115C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0000036; Molecular function: acyl carrier activity (inferred from electronic annotation from InterPro).
GO:0048037; Molecular function: cofactor binding (inferred from electronic annotation from InterPro).
GO:0004043; Molecular function: L-aminoadipate-semialdehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0016874; Molecular function: ligase activity (inferred from electronic annotation from InterPro).
GO:0031177; Molecular function: phosphopantetheine binding (inferred from electronic annotation from InterPro).
GO:0019878; Biological process: lysine biosynthetic process via aminoadipic acid (inferred from direct assay from SGD).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR010071; AA_adenyl_dom.
IPR000873; AMP-dep_Synth/Lig.
IPR014397; L-NH2adipate-semiAld_DH_lsu.
IPR013120; Male_sterile_NAD-bd.
IPR006163; Phsphopanteth_bd.
IPR006162; Ppantne_S.
IPR010080; Thioester_reductase.
Graphical view of domain structure.
Pfam PF00501; AMP-binding; 1.
PF07993; NAD_binding_4; 1.
PF00550; PP-binding; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001617; Alpha-AR; 1.
TIGRFAMs TIGR01733; AA-adenyl-dom; 1.
TIGR03443; alpha_am_amid; 1.
TIGR01746; Thioester-redct; 1.
PROSITE PS50075; ACP_DOMAIN; 1.
PS00455; AMP_BINDING; 1.
PS00012; PHOSPHOPANTETHEINE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P07702; -.
Genome annotation databases
Ensembl YBR115C; Saccharomyces cerevisiae. [Contig view]
GeneID 852412; -.
GenomeReviews Y13134_GR; YBR115C.
KEGG sce:YBR115C; -.
NMPDR fig|4932.3.peg.374; -.
Phylogenomic databases
HOGENOM P07702; -.
Other
LinkHub P07702; -.
NextBio 971264; -.
ProtoNet P07702.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1392  1392     L-aminoadipate-semialdehyde dehydrogenase. PRO_0000193153
DOMAIN   848    917  70     Acyl carrier. 
BINDING   880    880        Phosphopantetheine (covalent). 
MOD_RES   926    926        Phosphoserine. 
Sequence information
Length: 1392 AA [This is the length of the unprocessed precursor] Molecular weight: 155346 Da [This is the MW of the unprocessed precursor] CRC64: F0083A80BC6F7FB5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTNEKVWIEK LDNPTLSVLP HDFLRPQQEP YTKQATYSLQ LPQLDVPHDS FSNKYAVALS 

        70         80         90        100        110        120 
VWAALIYRVT GDDDIVLYIA NNKILRFNIQ PTWSFNELYS TINNELNKLN SIEANFSFDE 

       130        140        150        160        170        180 
LAEKIQSCQD LERTPQLFRL AFLENQDFKL DEFKHHLVDF ALNLDTSNNA HVLNLIYNSL 

       190        200        210        220        230        240 
LYSNERVTIV ADQFTQYLTA ALSDPSNCIT KISLITASSK DSLPDPTKNL GWCDFVGCIH 

       250        260        270        280        290        300 
DIFQDNAEAF PERTCVVETP TLNSDKSRSF TYRDINRTSN IVAHYLIKTG IKRGDVVMIY 

       310        320        330        340        350        360 
SSRGVDLMVC VMGVLKAGAT FSVIDPAYPP ARQTIYLGVA KPRGLIVIRA AGQLDQLVED 

       370        380        390        400        410        420 
YINDELEIVS RINSIAIQEN GTIEGGKLDN GEDVLAPYDH YKDTRTGVVV GPDSNPTLSF 

       430        440        450        460        470        480 
TSGSEGIPKG VLGRHFSLAY YFNWMSKRFN LTENDKFTML SGIAHDPIQR DMFTPLFLGA 

       490        500        510        520        530        540 
QLYVPTQDDI GTPGRLAEWM SKYGCTVTHL TPAMGQLLTA QATTPFPKLH HAFFVGDILT 

       550        560        570        580        590        600 
KRDCLRLQTL AENCRIVNMY GTTETQRAVS YFEVKSKNDD PNFLKKLKDV MPAGKGMLNV 

       610        620        630        640        650        660 
QLLVVNRNDR TQICGIGEIG EIYVRAGGLA EGYRGLPELN KEKFVNNWFV EKDHWNYLDK 

       670        680        690        700        710        720 
DNGEPWRQFW LGPRDRLYRT GDLGRYLPNG DCECCGRADD QVKIRGFRIE LGEIDTHISQ 

       730        740        750        760        770        780 
HPLVRENITL VRKNADNEPT LITFMVPRFD KPDDLSKFQS DVPKEVETDP IVKGLIGYHL 

       790        800        810        820        830        840 
LSKDIRTFLK KRLASYAMPS LIVVMDKLPL NPNGKVDKPK LQFPTPKQLN LVAENTVSET 

       850        860        870        880        890        900 
DDSQFTNVER EVRDLWLSIL PTKPASVSPD DSFFDLGGHS ILATKMIFTL KKKLQVDLPL 

       910        920        930        940        950        960 
GTIFKYPTIK AFAAEIDRIK SSGGSSQGEV VENVTANYAE DAKKLVETLP SSYPSREYFV 

       970        980        990       1000       1010       1020 
EPNSAEGKTT INVFVTGVTG FLGSYILADL LGRSPKNYSF KVFAHVRAKD EEAAFARLQK 

      1030       1040       1050       1060       1070       1080 
AGITYGTWNE KFASNIKVVL GDLSKSQFGL SDEKWMDLAN TVDIIIHNGA LVHWVYPYAK 

      1090       1100       1110       1120       1130       1140 
LRDPNVISTI NVMSLAAVGK PKFFDFVSST STLDTEYYFN LSDKLVSEGK PGILESDDLM 

      1150       1160       1170       1180       1190       1200 
NSASGLTGGY GQSKWAAEYI IRRAGERGLR GCIVRPGYVT GASANGSSNT DDFLLRFLKG 

      1210       1220       1230       1240       1250       1260 
SVQLGKIPDI ENSVNMVPVD HVARVVVATS LNPPKENELA VAQVTGHPRI LFKDYLYTLH 

      1270       1280       1290       1300       1310       1320 
DYGYDVEIES YSKWKKSLEA SVIDRNEENA LYPLLHMVLD NLPESTKAPE LDDRNAVASL 

      1330       1340       1350       1360       1370       1380 
KKDTAWTGVD WSNGIGVTPE EVGIYIAFLN KVGFLPPPTH NDKLPLPSIE LTQAQISLVA 

      1390 
SGAGARGSSA AA 

P07702 in FASTA format

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