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Protein

L-2-aminoadipate reductase

Gene

LYS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.1 Publication

Catalytic activityi

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.1 Publication
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate = L-2-aminoadipate + NADPH + ATP.1 Publication

Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 1 phosphopantetheine covalently.1 Publication

Kineticsi

kcat is 670 min(-1).1 Publication

Manual assertion based on experiment ini

  • Ref.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: FUNCTION, CATALYTIC ACTIVITY, PHOSPHOPANTETHEINYLATION AT SER-880, IDENTIFICATION BY MASS SPECTROMETRY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.

  1. KM=620 µM for NADPH1 Publication

    Pathwayi: L-lysine biosynthesis via AAA pathway

    This protein is involved in step 1 of the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route).
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-2-aminoadipate reductase (LYS2)
    2. Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] (LYS9)
    3. Saccharopine dehydrogenase [NAD(+), L-lysine-forming] (LYS1)
    This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lysine from L-alpha-aminoadipate (fungal route), the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    • 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

    BioCyciMetaCyc:YBR115C-MONOMER.
    YEAST:YBR115C-MONOMER.
    ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.
    R-SCE-193144. Estrogen biosynthesis.
    R-SCE-194002. Glucocorticoid biosynthesis.
    UniPathwayiUPA00033; UER00032.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-2-aminoadipate reductase (EC:1.2.1.311 Publication, EC:1.2.1.951 Publication)
    Alternative name(s):
    Alpha-aminoadipate reductase1 Publication
    Short name:
    Alpha-AR
    L-aminoadipate-semialdehyde dehydrogenase
    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
    Proteomesi
    • UP000002311 Componenti: Chromosome II

    Organism-specific databases

    EuPathDBiFungiDB:YBR115C.
    SGDiS000000319. LYS2.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: SGD
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001931531 – 1392L-2-aminoadipate reductaseAdd BLAST1392

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei880O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1
    Cross-linki1276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

    Keywords - PTMi

    Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP07702.
    PRIDEiP07702.

    PTM databases

    iPTMnetiP07702.

    Interactioni

    Protein-protein interaction databases

    BioGridi32818. 22 interactors.
    DIPiDIP-6811N.
    IntActiP07702. 4 interactors.
    MINTiMINT-661149.

    Structurei

    3D structure databases

    ProteinModelPortaliP07702.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini848 – 917Acyl carrierPROSITE-ProRule annotationAdd BLAST70

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00860000133667.
    HOGENOMiHOG000191209.
    InParanoidiP07702.
    KOiK00143.
    OMAiSYFVPDM.
    OrthoDBiEOG092C07V5.

    Family and domain databases

    CDDicd05235. SDR_e1. 1 hit.
    Gene3Di1.10.1200.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR010071. AA_adenyl_domain.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR014397. Lys2.
    IPR013120. Male_sterile_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    IPR020806. PKS_PP-bd.
    IPR009081. PP-bd_ACP.
    IPR006162. Ppantetheine_attach_site.
    IPR010080. Thioester_reductase-like_dom.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF07993. NAD_binding_4. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001617. Alpha-AR. 1 hit.
    SMARTiSM00823. PKS_PP. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF51735. SSF51735. 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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    ProteinModelPortaliP07702.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi32818. 22 interactors.
    DIPiDIP-6811N.
    IntActiP07702. 4 interactors.
    MINTiMINT-661149.

    PTM databases

    iPTMnetiP07702.

    Proteomic databases

    MaxQBiP07702.
    PRIDEiP07702.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:YBR115C.
    SGDiS000000319. LYS2.

    Phylogenomic databases

    GeneTreeiENSGT00860000133667.
    HOGENOMiHOG000191209.
    InParanoidiP07702.
    KOiK00143.
    OMAiSYFVPDM.
    OrthoDBiEOG092C07V5.

    Enzyme and pathway databases

    UniPathwayiUPA00033; UER00032.
    BioCyciMetaCyc:YBR115C-MONOMER.
    YEAST:YBR115C-MONOMER.
    ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.
    R-SCE-193144. Estrogen biosynthesis.
    R-SCE-194002. Glucocorticoid biosynthesis.

    Miscellaneous databases

    PROiP07702.

    Family and domain databases

    CDDicd05235. SDR_e1. 1 hit.
    Gene3Di1.10.1200.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR010071. AA_adenyl_domain.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    IPR014397. Lys2.
    IPR013120. Male_sterile_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    IPR020806. PKS_PP-bd.
    IPR009081. PP-bd_ACP.
    IPR006162. Ppantetheine_attach_site.
    IPR010080. Thioester_reductase-like_dom.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF07993. NAD_binding_4. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001617. Alpha-AR. 1 hit.
    SMARTiSM00823. PKS_PP. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF51735. SSF51735. 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]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 168 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.