Reviewed, UniProtKB/Swiss-Prot P07702 (LYS2_YEAST)

Names and origin

Protein names

Recommended name:
    L-aminoadipate-semialdehyde dehydrogenase
    EC=1.2.1.31
Alternative name(s):
    Alpha-aminoadipate reductase
      Short name=Alpha-AR

Gene names

Name:	LYS2
Ordered Locus Names:	YBR115C
ORF Names:	YBR0910

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1392 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH.
Catalytic activity	L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.
Cofactor	Binds 1 phosphopantetheine covalently.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungi route): step 1/3.
Miscellaneous	Present with 7430 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Lysine biosynthesis
Ligand	NADP Phosphopantetheine
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lysine biosynthetic process via aminoadipic acid Ref.7 Inferred from direct assay. Source: SGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	L-aminoadipate-semialdehyde dehydrogenase activity Ref.7 Inferred from direct assay. Source: SGD acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro ligase activity Inferred from electronic annotation. Source: InterPro phosphopantetheine binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1392	1392	L-aminoadipate-semialdehyde dehydrogenase		PRO_0000193153
Regions
	Domain	848 – 917	70	Acyl carrier
Amino acid modifications
	Modified residue	880	1	O-(pantetheine 4'-phosphoryl)serine
	Modified residue	926	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P07702-1 [UniParc]. Last modified March 1, 1992. Version 2. Checksum: F0083A80BC6F7FB5	FASTA	1,392	155,346
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae: homology to Bacillus brevis tyrocidine synthetase 1." Morris M.E., Jinks-Robertson S. Gene 98:141-145(1991) [PubMed: 2013406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of a 70 kb region on the right arm of yeast chromosome II." Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H. Yeast 10:1363-1381(1994) [PubMed: 7900426] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." 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. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Construction of LYS2 cartridges for use in genetic manipulations of Saccharomyces cerevisiae." Fleig U.N., Pridmore R.D., Philippsen P. Gene 46:237-245(1986) [PubMed: 3542721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 1209-1392.
[5]	"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." Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H. Yeast 8:397-408(1992) [PubMed: 1626431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1083-1392. Strain: ATCC 204508 / S288c.
[6]	"TKL2, a second transketolase gene of Saccharomyces cerevisiae. Cloning, sequence and deletion analysis of the gene." Schaaff-Gerstenschlaeger I., Mannhaupt G., Vetter I., Zimmermann F.K., Feldmann H. Eur. J. Biochem. 217:487-492(1993) [PubMed: 7916691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130. Strain: ATCC 204508 / S288c.
[7]	"Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5." Ehmann D.E., Gehring A.M., Walsh C.T. Biochemistry 38:6171-6177(1999) [PubMed: 10320345] [Abstract] Cited for: PHOSPHOPANTETHEINYLATION AT SER-880, MASS SPECTROMETRY.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M36287 Genomic DNA. Translation: AAA34747.1. X66247 Genomic DNA. Translation: CAA46975.1. X78993 Genomic DNA. Translation: CAA55617.1. Z35984 Genomic DNA. Translation: CAA85072.1. X73532 Genomic DNA. Translation: CAA51938.1.
PIR	YGBYAD. JU0448.
RefSeq	NP_009673.1.
3D structure databases
HSSP	HSSP built from PDB template 1DNY based on UniProtKB O30409.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6811N.
IntAct	P07702. 7 interactions.
Proteomic databases
PeptideAtlas	P07702.
Genome annotation databases
Ensembl	YBR115C. Saccharomyces cerevisiae. [Contig view]
GeneID	852412.
GenomeReviews	Gene locus YBR115C in contig Y13134_GR.
KEGG	sce:YBR115C.
NMPDR	fig|4932.3.peg.374.
Organism-specific databases
CYGD	YBR115c.
SGD	S000000319. LYS2.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P07702.
OMA	P07702. THLTPAM.
Enzyme and pathway databases
BRENDA	1.2.1.31. 250.
Gene expression databases
ArrayExpress	P07702.
GermOnline	YBR115C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR010071. AA_adenyl_domain. IPR009081. Acyl_carrier_prot-like. 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]
Pfam	PF00501. AMP-binding. 1 hit. PF07993. NAD_binding_4. 1 hit. PF00550. PP-binding. 1 hit. [Graphical view]
PIRSF	PIRSF001617. Alpha-AR. 1 hit.
TIGRFAMs	TIGR01733. AA-adenyl-dom. 1 hit. TIGR03443. alpha_am_amid. 1 hit. TIGR01746. Thioester-redct. 1 hit.
PROSITE	PS50075. ACP_DOMAIN. 1 hit. PS00455. AMP_BINDING. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	971264.

Entry information

Entry name

LYS2_YEAST

Accession

Primary (citable) accession number: P07702

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	March 1, 1992
Last modified:	June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)