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P40976

- LYS2_SCHPO

UniProt

P40976 - LYS2_SCHPO

Protein

L-aminoadipate-semialdehyde dehydrogenase

Gene

lys1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 3 (21 Feb 2001)
      Previous versions | rss
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    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.Curated

    Pathwayi

    GO - Molecular functioni

    1. fatty-acyl-CoA binding Source: PomBase
    2. L-aminoadipate-semialdehyde dehydrogenase activity Source: PomBase
    3. phosphopantetheine binding Source: InterPro

    GO - Biological processi

    1. lysine biosynthetic process Source: PomBase
    2. lysine biosynthetic process via aminoadipic acid Source: PomBase
    3. negative regulation of lysine biosynthetic process via aminoadipic acid Source: PomBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    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:lys1
    ORF Names:SPAP7G5.04c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAP7G5.04c.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: PomBase
    2. cytosol Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi913 – 9131G → A: No activity. 1 Publication
    Mutagenesisi916 – 9161S → A or T: No activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14191419L-aminoadipate-semialdehyde dehydrogenasePRO_0000193152Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei916 – 9161O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Proteomic databases

    MaxQBiP40976.
    PaxDbiP40976.

    Interactioni

    Protein-protein interaction databases

    BioGridi278556. 3 interactions.
    MINTiMINT-4689880.
    STRINGi4896.SPAP7G5.04c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP40976.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini885 – 95369Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3320.
    HOGENOMiHOG000191209.
    KOiK00143.
    OMAiDRFTMLS.
    OrthoDBiEOG74TX6Z.
    PhylomeDBiP40976.

    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.

    P40976-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTAPSDTE YNQRLERWSE RLKSQTISHL PTDYSRPVPS RLVEAVFERT     50
    LPEDAKTALI KVYVAAQAKG ILVTPFNILL TIFIILVSRM TGDEDISIGT 100
    SSENAIPFVL RTFIQPSDSF LDLLAKVCDL EKEGSSDAVD FSDLINFLNA 150
    KLSKKDDPRK TLVHLRFYNA PDAPSENFLS TTGLDVDLTV LVSVKKPSDQ 200
    LTSLRSQFTF PDLQLKLIYN QLLFSESRVN IVADQLLKLV VSASKDVTGP 250
    IGALDLMTPT QMNVLPDPTV DLDWSGYRGA IQDIFASNAA KFPDRECIVV 300
    TPSVTIDAPV TSYTYRQIDE SSNILAHHLV KNGIERGDVV MVYAYRGVDL 350
    VVAVMGVLKA GATFSVIDPA YPPARQIIYL SVAKPRALVV LEDAGVLSPT 400
    VVEYVEKSLE LKTYVPALKL AKDGSLTGGS VSKGADDILQ HVLHLKSEQT 450
    GVVVGPDSTP TLSFTSGSEG IPKGVKGRHF SLAYYFDWMA QEFNLSESDR 500
    FTMLSGIAHD PIQRDIFTPL FLGASLIVPT AEDIGTPGQL AQWANKYKVT 550
    VTHLTPAMGQ LLAAQADEPI PSLHHAFFVG DILTKRDCLR LQVLANNVNV 600
    VNMYGTTETQ RSVSYFVVPA RSQDQTFLES QKDVIPAGRG MKNVQLLVIN 650
    RFDTNKICGI GEVGEIYLRA GGLAEGYLGN DELTSKKFLK SWFADPSKFV 700
    DRTPENAPWK PYWFGIRDRM YRSGDLGRYL PTGNVECSGR ADDQIKIRGF 750
    RIELGEINTH LSRHPNVREN ITLVRRDKDE EPTLVAYIVP QGLNKDDFDS 800
    ATESEDIVVN GLKKYRKLIH DIREYLKTKL PSYAIPSVIV PLHKMPLNPN 850
    GKIDKPALPF PDTSQLAAAS RSHSKHGVDE TLTATERDIR DIWLRIIPHA 900
    TDVNKKASFF DIGGHSILAT RLIFELRKKF AVNVPLGLVF SEPTIEGLAK 950
    EIERMKSGEM ISVMDIGKEE TREPEIEYGK DALDLVDLIP KEFPTSKDLG 1000
    IDEPKTVFLT GANGYLGVFI LRDLMTRSSN LKVIALVRAS SEEHGLKRLK 1050
    DSCTAYGVWD ESWAQKISVV NGDLALENWG IEERKWNKLT EVVDYVIHNG 1100
    ALVHWVYPYS KLRGPNVMGT ITALKLCSLG KGKSLSFVSS TSTVDTEYYV 1150
    NLSNEITSKG GNGIPESDPL QGSSKDLHTG YGQSKWVSEY LVRQAGLRGL 1200
    RGVVVRPGYI LGDSKSGAIN TDDFLVRMVK GCIELGLYPN INNTVNMVPA 1250
    DHVARVVTAS AFHPEQGVIV AHVTSHPRLR FNQFLGTLST FGFNTKLSEY 1300
    VNWRIALERF VINESHDSAL YPLLHFVLDN LPANTKAPEL DDTNTREILK 1350
    RDASWTNVDV SNGAAILEHE MGLYLSYLVA IGFLPKPTLE GKKLPEVKIN 1400
    EATLEKLASA GGRGGAPTH 1419
    Length:1,419
    Mass (Da):156,894
    Last modified:February 21, 2001 - v3
    Checksum:i09AFBEFE09F21A0C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 912MT → IA in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti196 – 1961Missing in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti487 – 4871D → DG in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti500 – 5001R → G in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti600 – 6023Missing in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti620 – 6212AR → GP in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti712 – 7121Y → S in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti926 – 9283LRK → PSQ in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti1203 – 12053VVV → AAA in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti1225 – 12284LVRM → WSK in AAC15909. (PubMed:8590464)Curated
    Sequence conflicti1239 – 12391P → A in AAC15909. (PubMed:8590464)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15923 Genomic DNA. Translation: AAC15909.1.
    CU329670 Genomic DNA. Translation: CAB88271.1.
    PIRiS57264.
    RefSeqiNP_594314.1. NM_001019737.2.

    Genome annotation databases

    EnsemblFungiiSPAP7G5.04c.1; SPAP7G5.04c.1:pep; SPAP7G5.04c.
    GeneIDi2542079.
    KEGGispo:SPAP7G5.04c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15923 Genomic DNA. Translation: AAC15909.1 .
    CU329670 Genomic DNA. Translation: CAB88271.1 .
    PIRi S57264.
    RefSeqi NP_594314.1. NM_001019737.2.

    3D structure databases

    ProteinModelPortali P40976.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 278556. 3 interactions.
    MINTi MINT-4689880.
    STRINGi 4896.SPAP7G5.04c-1.

    Proteomic databases

    MaxQBi P40976.
    PaxDbi P40976.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAP7G5.04c.1 ; SPAP7G5.04c.1:pep ; SPAP7G5.04c .
    GeneIDi 2542079.
    KEGGi spo:SPAP7G5.04c.

    Organism-specific databases

    PomBasei SPAP7G5.04c.

    Phylogenomic databases

    eggNOGi COG3320.
    HOGENOMi HOG000191209.
    KOi K00143.
    OMAi DRFTMLS.
    OrthoDBi EOG74TX6Z.
    PhylomeDBi P40976.

    Enzyme and pathway databases

    UniPathwayi UPA00033 ; UER00032 .

    Miscellaneous databases

    NextBioi 20803152.

    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

    1. "Molecular properties of the lys1+ gene and the regulation of alpha-aminoadipate reductase in Schizosaccharomyces pombe."
      Ford R.A., Bhattacharjee J.K.
      Curr. Genet. 28:131-137(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe."
      Guo S., Bhattacharjee J.K.
      Yeast 21:1279-1288(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-913 AND SER-916.
      Strain: 972 / ATCC 24843.
    4. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
      Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
      Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLYS2_SCHPO
    AccessioniPrimary (citable) accession number: P40976
    Secondary accession number(s): Q9P770
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 21, 2001
    Last modified: October 1, 2014
    This is version 123 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3