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P07702

- LYS2_YEAST

UniProt

P07702 - LYS2_YEAST

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Protein

L-aminoadipate-semialdehyde dehydrogenase

Gene

LYS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH.

Catalytic activityi

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.

Cofactori

Binds 1 phosphopantetheine covalently.

Pathwayi

GO - Molecular functioni

  1. L-aminoadipate-semialdehyde dehydrogenase activity Source: SGD
  2. phosphopantetheine binding Source: InterPro

GO - Biological processi

  1. lysine biosynthetic process via aminoadipic acid Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:YBR115C-MONOMER.
UniPathwayiUPA00033; UER00032.

Names & Taxonomyi

Protein namesi
Recommended name:
L-aminoadipate-semialdehyde dehydrogenase (EC:1.2.1.31)
Alternative name(s):
Alpha-aminoadipate reductase
Short name:
Alpha-AR
Gene namesi
Name:LYS2
Ordered Locus Names:YBR115C
ORF Names:YBR0910
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR115c.
SGDiS000000319. LYS2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13921392L-aminoadipate-semialdehyde dehydrogenasePRO_0000193153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei880 – 8801O-(pantetheine 4'-phosphoryl)serine1 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

MaxQBiP07702.
PaxDbiP07702.
PeptideAtlasiP07702.

Expressioni

Gene expression databases

GenevestigatoriP07702.

Interactioni

Protein-protein interaction databases

BioGridi32818. 23 interactions.
DIPiDIP-6811N.
IntActiP07702. 4 interactions.
MINTiMINT-661149.
STRINGi4932.YBR115C.

Structurei

3D structure databases

ProteinModelPortaliP07702.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini848 – 91770Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3320.
GeneTreeiENSGT00760000118798.
HOGENOMiHOG000191209.
InParanoidiP07702.
KOiK00143.
OMAiDRFTMLS.
OrthoDBiEOG74TX6Z.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR014397. L-NH2adipate-semiAld_DH_lsu.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR006162. PPantetheine_attach_site.
IPR010080. Thioester_reductase-like_dom.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF001617. Alpha-AR. 1 hit.
SUPFAMiSSF47336. SSF47336. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
TIGR03443. alpha_am_amid. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07702-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNEKVWIEK LDNPTLSVLP HDFLRPQQEP YTKQATYSLQ LPQLDVPHDS
60 70 80 90 100
FSNKYAVALS VWAALIYRVT GDDDIVLYIA NNKILRFNIQ PTWSFNELYS
110 120 130 140 150
TINNELNKLN SIEANFSFDE LAEKIQSCQD LERTPQLFRL AFLENQDFKL
160 170 180 190 200
DEFKHHLVDF ALNLDTSNNA HVLNLIYNSL LYSNERVTIV ADQFTQYLTA
210 220 230 240 250
ALSDPSNCIT KISLITASSK DSLPDPTKNL GWCDFVGCIH DIFQDNAEAF
260 270 280 290 300
PERTCVVETP TLNSDKSRSF TYRDINRTSN IVAHYLIKTG IKRGDVVMIY
310 320 330 340 350
SSRGVDLMVC VMGVLKAGAT FSVIDPAYPP ARQTIYLGVA KPRGLIVIRA
360 370 380 390 400
AGQLDQLVED YINDELEIVS RINSIAIQEN GTIEGGKLDN GEDVLAPYDH
410 420 430 440 450
YKDTRTGVVV GPDSNPTLSF TSGSEGIPKG VLGRHFSLAY YFNWMSKRFN
460 470 480 490 500
LTENDKFTML SGIAHDPIQR DMFTPLFLGA QLYVPTQDDI GTPGRLAEWM
510 520 530 540 550
SKYGCTVTHL TPAMGQLLTA QATTPFPKLH HAFFVGDILT KRDCLRLQTL
560 570 580 590 600
AENCRIVNMY GTTETQRAVS YFEVKSKNDD PNFLKKLKDV MPAGKGMLNV
610 620 630 640 650
QLLVVNRNDR TQICGIGEIG EIYVRAGGLA EGYRGLPELN KEKFVNNWFV
660 670 680 690 700
EKDHWNYLDK DNGEPWRQFW LGPRDRLYRT GDLGRYLPNG DCECCGRADD
710 720 730 740 750
QVKIRGFRIE LGEIDTHISQ HPLVRENITL VRKNADNEPT LITFMVPRFD
760 770 780 790 800
KPDDLSKFQS DVPKEVETDP IVKGLIGYHL LSKDIRTFLK KRLASYAMPS
810 820 830 840 850
LIVVMDKLPL NPNGKVDKPK LQFPTPKQLN LVAENTVSET DDSQFTNVER
860 870 880 890 900
EVRDLWLSIL PTKPASVSPD DSFFDLGGHS ILATKMIFTL KKKLQVDLPL
910 920 930 940 950
GTIFKYPTIK AFAAEIDRIK SSGGSSQGEV VENVTANYAE DAKKLVETLP
960 970 980 990 1000
SSYPSREYFV EPNSAEGKTT INVFVTGVTG FLGSYILADL LGRSPKNYSF
1010 1020 1030 1040 1050
KVFAHVRAKD EEAAFARLQK AGITYGTWNE KFASNIKVVL GDLSKSQFGL
1060 1070 1080 1090 1100
SDEKWMDLAN TVDIIIHNGA LVHWVYPYAK LRDPNVISTI NVMSLAAVGK
1110 1120 1130 1140 1150
PKFFDFVSST STLDTEYYFN LSDKLVSEGK PGILESDDLM NSASGLTGGY
1160 1170 1180 1190 1200
GQSKWAAEYI IRRAGERGLR GCIVRPGYVT GASANGSSNT DDFLLRFLKG
1210 1220 1230 1240 1250
SVQLGKIPDI ENSVNMVPVD HVARVVVATS LNPPKENELA VAQVTGHPRI
1260 1270 1280 1290 1300
LFKDYLYTLH DYGYDVEIES YSKWKKSLEA SVIDRNEENA LYPLLHMVLD
1310 1320 1330 1340 1350
NLPESTKAPE LDDRNAVASL KKDTAWTGVD WSNGIGVTPE EVGIYIAFLN
1360 1370 1380 1390
KVGFLPPPTH NDKLPLPSIE LTQAQISLVA SGAGARGSSA AA
Length:1,392
Mass (Da):155,346
Last modified:March 1, 1992 - v2
Checksum:iF0083A80BC6F7FB5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BK006936 Genomic DNA. Translation: DAA07234.1.
PIRiJU0448. YGBYAD.
RefSeqiNP_009673.1. NM_001178463.1.

Genome annotation databases

EnsemblFungiiYBR115C; YBR115C; YBR115C.
GeneIDi852412.
KEGGisce:YBR115C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
BK006936 Genomic DNA. Translation: DAA07234.1 .
PIRi JU0448. YGBYAD.
RefSeqi NP_009673.1. NM_001178463.1.

3D structure databases

ProteinModelPortali P07702.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32818. 23 interactions.
DIPi DIP-6811N.
IntActi P07702. 4 interactions.
MINTi MINT-661149.
STRINGi 4932.YBR115C.

Proteomic databases

MaxQBi P07702.
PaxDbi P07702.
PeptideAtlasi P07702.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR115C ; YBR115C ; YBR115C .
GeneIDi 852412.
KEGGi sce:YBR115C.

Organism-specific databases

CYGDi YBR115c.
SGDi S000000319. LYS2.

Phylogenomic databases

eggNOGi COG3320.
GeneTreei ENSGT00760000118798.
HOGENOMi HOG000191209.
InParanoidi P07702.
KOi K00143.
OMAi DRFTMLS.
OrthoDBi EOG74TX6Z.

Enzyme and pathway databases

UniPathwayi UPA00033 ; UER00032 .
BioCyci YEAST:YBR115C-MONOMER.

Miscellaneous databases

NextBioi 971264.

Gene expression databases

Genevestigatori P07702.

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR014397. L-NH2adipate-semiAld_DH_lsu.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR006162. PPantetheine_attach_site.
IPR010080. Thioester_reductase-like_dom.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view ]
PIRSFi PIRSF001617. Alpha-AR. 1 hit.
SUPFAMi SSF47336. SSF47336. 1 hit.
TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
TIGR03443. alpha_am_amid. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 1209-1392.
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1083-1392.
    Strain: ATCC 204508 / S288c.
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
    Strain: ATCC 204508 / S288c.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHOPANTETHEINYLATION AT SER-880, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLYS2_YEAST
AccessioniPrimary (citable) accession number: P07702
Secondary accession number(s): D6VQB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: March 1, 1992
Last modified: October 29, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7430 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3