ID   LYS2_YEAST              Reviewed;        1392 AA.
AC   P07702;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   16-JUN-2009, entry version 100.
DE   RecName: Full=L-aminoadipate-semialdehyde dehydrogenase;
DE            EC=1.2.1.31;
DE   AltName: Full=Alpha-aminoadipate reductase;
DE            Short=Alpha-AR;
GN   Name=LYS2; OrderedLocusNames=YBR115C; ORFNames=YBR0910;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91192607; PubMed=2013406; DOI=10.1016/0378-1119(91)90117-T;
RA   Morris M.E., Jinks-Robertson S.;
RT   "Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae:
RT   homology to Bacillus brevis tyrocidine synthetase 1.";
RL   Gene 98:141-145(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=95208357; PubMed=7900426; DOI=10.1002/yea.320101014;
RA   Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT   "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL   Yeast 10:1363-1381(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=95112788; PubMed=7813418;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 1209-1392.
RX   MEDLINE=87106859; PubMed=3542721; DOI=10.1016/0378-1119(86)90408-7;
RA   Fleig U.N., Pridmore R.D., Philippsen P.;
RT   "Construction of LYS2 cartridges for use in genetic manipulations of
RT   Saccharomyces cerevisiae.";
RL   Gene 46:237-245(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1083-1392.
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=92327848; PubMed=1626431; DOI=10.1002/yea.320080507;
RA   Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT   "Molecular analysis of yeast chromosome II between CMD1 and LYS2: the
RT   excision repair gene RAD16 located in this region belongs to a novel
RT   group of double-finger proteins.";
RL   Yeast 8:397-408(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=94039074; PubMed=7916691;
RX   DOI=10.1111/j.1432-1033.1993.tb18268.x;
RA   Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K.,
RA   Feldmann H.;
RT   "TKL2, a second transketolase gene of Saccharomyces cerevisiae.
RT   Cloning, sequence and deletion analysis of the gene.";
RL   Eur. J. Biochem. 217:487-492(1993).
RN   [7]
RP   PHOSPHOPANTETHEINYLATION AT SER-880, AND MASS SPECTROMETRY.
RX   PubMed=10320345; DOI=10.1021/bi9829940;
RA   Ehmann D.E., Gehring A.M., Walsh C.T.;
RT   "Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-
RT   aminoadipate reductase (Lys2) involves posttranslational
RT   phosphopantetheinylation by Lys5.";
RL   Biochemistry 38:6171-6177(1999).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Catalyzes the activation of alpha-aminoadipate by ATP-
CC       dependent adenylation and the reduction of activated alpha-
CC       aminoadipate by NADPH.
CC   -!- CATALYTIC ACTIVITY: L-2-aminoadipate 6-semialdehyde + NAD(P)(+) +
CC       H(2)O = L-2-aminoadipate + NAD(P)H.
CC   -!- COFACTOR: Binds 1 phosphopantetheine covalently.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungi route): step
CC       1/3.
CC   -!- MISCELLANEOUS: Present with 7430 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
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DR   EMBL; M36287; AAA34747.1; -; Genomic_DNA.
DR   EMBL; X66247; CAA46975.1; -; Genomic_DNA.
DR   EMBL; X78993; CAA55617.1; -; Genomic_DNA.
DR   EMBL; Z35984; CAA85072.1; -; Genomic_DNA.
DR   EMBL; X73532; CAA51938.1; -; Genomic_DNA.
DR   PIR; JU0448; YGBYAD.
DR   RefSeq; NP_009673.1; -.
DR   HSSP; O30409; 1DNY.
DR   DIP; DIP:6811N; -.
DR   IntAct; P07702; 7.
DR   PeptideAtlas; P07702; -.
DR   Ensembl; YBR115C; Saccharomyces cerevisiae.
DR   GeneID; 852412; -.
DR   GenomeReviews; Y13134_GR; YBR115C.
DR   KEGG; sce:YBR115C; -.
DR   NMPDR; fig|4932.3.peg.374; -.
DR   CYGD; YBR115c; -.
DR   SGD; S000000319; LYS2.
DR   HOGENOM; P07702; -.
DR   OMA; P07702; THLTPAM.
DR   BRENDA; 1.2.1.31; 250.
DR   NextBio; 971264; -.
DR   ArrayExpress; P07702; -.
DR   GermOnline; YBR115C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase a...; IDA:SGD.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic...; IDA:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR014397; L-NH2adipate-semiAld_DH_lsu.
DR   InterPro; IPR013120; Male_sterile_NAD-bd.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR006162; Ppantne_S.
DR   InterPro; IPR010080; Thioester_reductase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 1.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   TIGRFAMs; TIGR03443; alpha_am_amid; 1.
DR   TIGRFAMs; TIGR01746; Thioester-redct; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; Lysine biosynthesis; NADP;
KW   Oxidoreductase; Phosphopantetheine; Phosphoprotein.
FT   CHAIN         1   1392       L-aminoadipate-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000193153.
FT   DOMAIN      848    917       Acyl carrier.
FT   MOD_RES     880    880       O-(pantetheine 4'-phosphoryl)serine.
FT   MOD_RES     926    926       Phosphoserine.
SQ   SEQUENCE   1392 AA;  155346 MW;  F0083A80BC6F7FB5 CRC64;
     MTNEKVWIEK LDNPTLSVLP HDFLRPQQEP YTKQATYSLQ LPQLDVPHDS FSNKYAVALS
     VWAALIYRVT GDDDIVLYIA NNKILRFNIQ PTWSFNELYS TINNELNKLN SIEANFSFDE
     LAEKIQSCQD LERTPQLFRL AFLENQDFKL DEFKHHLVDF ALNLDTSNNA HVLNLIYNSL
     LYSNERVTIV ADQFTQYLTA ALSDPSNCIT KISLITASSK DSLPDPTKNL GWCDFVGCIH
     DIFQDNAEAF PERTCVVETP TLNSDKSRSF TYRDINRTSN IVAHYLIKTG IKRGDVVMIY
     SSRGVDLMVC VMGVLKAGAT FSVIDPAYPP ARQTIYLGVA KPRGLIVIRA AGQLDQLVED
     YINDELEIVS RINSIAIQEN GTIEGGKLDN GEDVLAPYDH YKDTRTGVVV GPDSNPTLSF
     TSGSEGIPKG VLGRHFSLAY YFNWMSKRFN LTENDKFTML SGIAHDPIQR DMFTPLFLGA
     QLYVPTQDDI GTPGRLAEWM SKYGCTVTHL TPAMGQLLTA QATTPFPKLH HAFFVGDILT
     KRDCLRLQTL AENCRIVNMY GTTETQRAVS YFEVKSKNDD PNFLKKLKDV MPAGKGMLNV
     QLLVVNRNDR TQICGIGEIG EIYVRAGGLA EGYRGLPELN KEKFVNNWFV EKDHWNYLDK
     DNGEPWRQFW LGPRDRLYRT GDLGRYLPNG DCECCGRADD QVKIRGFRIE LGEIDTHISQ
     HPLVRENITL VRKNADNEPT LITFMVPRFD KPDDLSKFQS DVPKEVETDP IVKGLIGYHL
     LSKDIRTFLK KRLASYAMPS LIVVMDKLPL NPNGKVDKPK LQFPTPKQLN LVAENTVSET
     DDSQFTNVER EVRDLWLSIL PTKPASVSPD DSFFDLGGHS ILATKMIFTL KKKLQVDLPL
     GTIFKYPTIK AFAAEIDRIK SSGGSSQGEV VENVTANYAE DAKKLVETLP SSYPSREYFV
     EPNSAEGKTT INVFVTGVTG FLGSYILADL LGRSPKNYSF KVFAHVRAKD EEAAFARLQK
     AGITYGTWNE KFASNIKVVL GDLSKSQFGL SDEKWMDLAN TVDIIIHNGA LVHWVYPYAK
     LRDPNVISTI NVMSLAAVGK PKFFDFVSST STLDTEYYFN LSDKLVSEGK PGILESDDLM
     NSASGLTGGY GQSKWAAEYI IRRAGERGLR GCIVRPGYVT GASANGSSNT DDFLLRFLKG
     SVQLGKIPDI ENSVNMVPVD HVARVVVATS LNPPKENELA VAQVTGHPRI LFKDYLYTLH
     DYGYDVEIES YSKWKKSLEA SVIDRNEENA LYPLLHMVLD NLPESTKAPE LDDRNAVASL
     KKDTAWTGVD WSNGIGVTPE EVGIYIAFLN KVGFLPPPTH NDKLPLPSIE LTQAQISLVA
     SGAGARGSSA AA
//