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Protein

AMP nucleosidase

Gene

amn

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations.UniRule annotation1 Publication

Catalytic activityi

AMP + H2O = D-ribose 5-phosphate + adenine.UniRule annotation1 Publication

Enzyme regulationi

Allosterically activated by Mg-ATP. Inhibited by inorganic phosphate and formycin monophosphate.1 Publication

Kineticsi

  1. KM=15 mM for AMP (in the absence of Mg-ATP)1 Publication
  2. KM=0.09 mM for AMP (in the presence of saturating Mg-ATP)1 Publication

    GO - Molecular functioni

    • AMP nucleosidase activity Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:AMP-NUCLEOSID-MONOMER.
    ECOL316407:JW1963-MONOMER.
    MetaCyc:AMP-NUCLEOSID-MONOMER.
    RETL1328306-WGS:GSTH-1334-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP nucleosidase1 PublicationUniRule annotation (EC:3.2.2.4UniRule annotation1 Publication)
    Gene namesi
    Name:amn1 PublicationUniRule annotation
    Ordered Locus Names:b1982Imported, JW1963Imported
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10039. amn.

    Pathology & Biotechi

    Disruption phenotypei

    Knockout elevates intracellular ATP levels and increases cold tolerance.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484AMP nucleosidasePRO_0000064586Add
    BLAST

    Proteomic databases

    PaxDbiP0AE12.
    PRIDEiP0AE12.

    Expressioni

    Inductioni

    By cAMP at limiting phosphate concentrations. Repressed by phosphate.1 Publication

    Gene expression databases

    GenevestigatoriP0AE12.

    Interactioni

    Subunit structurei

    Homohexamer. Trimer of dimers.1 Publication

    Protein-protein interaction databases

    IntActiP0AE12. 8 interactions.
    STRINGi511145.b1982.

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 3829Combined sources
    Helixi44 – 474Combined sources
    Turni48 – 503Combined sources
    Beta strandi51 – 6111Combined sources
    Beta strandi73 – 753Combined sources
    Beta strandi78 – 869Combined sources
    Turni90 – 934Combined sources
    Helixi94 – 10815Combined sources
    Beta strandi111 – 12010Combined sources
    Helixi123 – 1264Combined sources
    Helixi136 – 14510Combined sources
    Beta strandi169 – 1746Combined sources
    Helixi176 – 19015Combined sources
    Helixi194 – 1963Combined sources
    Beta strandi199 – 2057Combined sources
    Helixi208 – 22215Combined sources
    Beta strandi226 – 2338Combined sources
    Beta strandi238 – 2403Combined sources
    Helixi246 – 2483Combined sources
    Helixi254 – 2574Combined sources
    Beta strandi262 – 2676Combined sources
    Beta strandi273 – 2775Combined sources
    Helixi282 – 29211Combined sources
    Helixi293 – 2953Combined sources
    Beta strandi298 – 3025Combined sources
    Beta strandi305 – 3084Combined sources
    Beta strandi318 – 32710Combined sources
    Turni330 – 3345Combined sources
    Helixi345 – 35814Combined sources
    Helixi363 – 3686Combined sources
    Beta strandi370 – 37910Combined sources
    Helixi383 – 3864Combined sources
    Helixi387 – 39711Combined sources
    Beta strandi399 – 4057Combined sources
    Helixi406 – 41510Combined sources
    Beta strandi420 – 4289Combined sources
    Helixi430 – 4323Combined sources
    Helixi443 – 4464Combined sources
    Helixi448 – 46518Combined sources
    Turni466 – 4705Combined sources
    Helixi473 – 4753Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T8RX-ray2.70A/B/C/D/E/F1-484[»]
    1T8SX-ray2.60A/B/C/D/E/F1-484[»]
    1T8WX-ray2.80A/B/C/D/E/F1-484[»]
    1T8YX-ray3.00A/B/C/D/E/F1-484[»]
    ProteinModelPortaliP0AE12.
    SMRiP0AE12. Positions 8-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AE12.

    Family & Domainsi

    Domaini

    Each monomer consists of two domains: a C-terminal catalytic domain and a putative N-terminal regulatory domain.1 Publication

    Sequence similaritiesi

    Belongs to the AMP nucleosidase family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiCOG0775.
    HOGENOMiHOG000156781.
    InParanoidiP0AE12.
    KOiK01241.
    OMAiAYVREDH.
    OrthoDBiEOG67DPGS.
    PhylomeDBiP0AE12.

    Family and domain databases

    Gene3Di3.30.1730.10. 1 hit.
    3.40.50.1580. 1 hit.
    HAMAPiMF_01932. AMP_nucleosidase.
    InterProiIPR011271. AMP_nucleosidase.
    IPR018953. AMP_nucleoside_Pase_N.
    IPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 1 hit.
    PfamiPF10423. AMNp_N. 1 hit.
    PF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01717. AMP-nucleosdse. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AE12-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNNKGSGLTP AQALDKLDAL YEQSVVALRN AIGNYITSGE LPDENARKQG
    60 70 80 90 100
    LFVYPSLTVT WDGSTTNPPK TRAFGRFTHA GSYTTTITRP TLFRSYLNEQ
    110 120 130 140 150
    LTLLYQDYGA HISVQPSQHE IPYPYVIDGS ELTLDRSMSA GLTRYFPTTE
    160 170 180 190 200
    LAQIGDETAD GIYHPTEFSP LSHFDARRVD FSLARLRHYT GTPVEHFQPF
    210 220 230 240 250
    VLFTNYTRYV DEFVRWGCSQ ILDPDSPYIA LSCAGGNWIT AETEAPEEAI
    260 270 280 290 300
    SDLAWKKHQM PAWHLITADG QGITLVNIGV GPSNAKTICD HLAVLRPDVW
    310 320 330 340 350
    LMIGHCGGLR ESQAIGDYVL AHAYLRDDHV LDAVLPPDIP IPSIAEVQRA
    360 370 380 390 400
    LYDATKLVSG RPGEEVKQRL RTGTVVTTDD RNWELRYSAS ALRFNLSRAV
    410 420 430 440 450
    AIDMESATIA AQGYRFRVPY GTLLCVSDKP LHGEIKLPGQ ANRFYEGAIS
    460 470 480
    EHLQIGIRAI DLLRAEGDRL HSRKLRTFNE PPFR
    Length:484
    Mass (Da):53,995
    Last modified:December 6, 2005 - v1
    Checksum:iADC2FD95CC220527
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti300 – 3023WLM → CY in AAA23433 (PubMed:2690948).Curated
    Sequence conflicti311 – 3166ESQAIG → KVRPLA in AAA23433 (PubMed:2690948).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M30469 Genomic DNA. Translation: AAA23433.1.
    U00096 Genomic DNA. Translation: AAC75046.1.
    AP009048 Genomic DNA. Translation: BAA15802.1.
    U88529 Genomic DNA. Translation: AAC46272.1.
    PIRiH64962.
    RefSeqiNP_416489.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC75046; AAC75046; b1982.
    BAA15802; BAA15802; BAA15802.
    GeneIDi946508.
    KEGGiecj:Y75_p1946.
    eco:b1982.
    PATRICi32119295. VBIEscCol129921_2060.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M30469 Genomic DNA. Translation: AAA23433.1.
    U00096 Genomic DNA. Translation: AAC75046.1.
    AP009048 Genomic DNA. Translation: BAA15802.1.
    U88529 Genomic DNA. Translation: AAC46272.1.
    PIRiH64962.
    RefSeqiNP_416489.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T8RX-ray2.70A/B/C/D/E/F1-484[»]
    1T8SX-ray2.60A/B/C/D/E/F1-484[»]
    1T8WX-ray2.80A/B/C/D/E/F1-484[»]
    1T8YX-ray3.00A/B/C/D/E/F1-484[»]
    ProteinModelPortaliP0AE12.
    SMRiP0AE12. Positions 8-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP0AE12. 8 interactions.
    STRINGi511145.b1982.

    Proteomic databases

    PaxDbiP0AE12.
    PRIDEiP0AE12.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75046; AAC75046; b1982.
    BAA15802; BAA15802; BAA15802.
    GeneIDi946508.
    KEGGiecj:Y75_p1946.
    eco:b1982.
    PATRICi32119295. VBIEscCol129921_2060.

    Organism-specific databases

    EchoBASEiEB0037.
    EcoGeneiEG10039. amn.

    Phylogenomic databases

    eggNOGiCOG0775.
    HOGENOMiHOG000156781.
    InParanoidiP0AE12.
    KOiK01241.
    OMAiAYVREDH.
    OrthoDBiEOG67DPGS.
    PhylomeDBiP0AE12.

    Enzyme and pathway databases

    BioCyciEcoCyc:AMP-NUCLEOSID-MONOMER.
    ECOL316407:JW1963-MONOMER.
    MetaCyc:AMP-NUCLEOSID-MONOMER.
    RETL1328306-WGS:GSTH-1334-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0AE12.
    PROiP0AE12.

    Gene expression databases

    GenevestigatoriP0AE12.

    Family and domain databases

    Gene3Di3.30.1730.10. 1 hit.
    3.40.50.1580. 1 hit.
    HAMAPiMF_01932. AMP_nucleosidase.
    InterProiIPR011271. AMP_nucleosidase.
    IPR018953. AMP_nucleoside_Pase_N.
    IPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 1 hit.
    PfamiPF10423. AMNp_N. 1 hit.
    PF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01717. AMP-nucleosdse. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli."
      Leung H.B., Kvalnes-Krick K.L., Meyer S.L., Deriel J.K., Schramm V.L.
      Biochemistry 28:8726-8733(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, INDUCTION.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Cloning and analysis of the shiA gene, which encodes the shikimate transport system of Escherichia coli K-12."
      Whipp M.J., Camakaris H., Pittard A.J.
      Gene 209:185-192(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
      Strain: K12.
    6. "Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme."
      Leung H.B., Schramm V.L.
      J. Biol. Chem. 255:10867-10874(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "An AMP nucleosidase gene knockout in Escherichia coli elevates intracellular ATP levels and increases cold tolerance."
      Morrison B.A., Shain D.H.
      Biol. Lett. 4:53-56(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    9. "Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases."
      Zhang Y., Cottet S.E., Ealick S.E.
      Structure 12:1383-1394(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FORMYCIN-5'-MONOPHOSPHATE AND PHOSPHATE, SUBUNIT, DOMAIN.

    Entry informationi

    Entry nameiAMN_ECOLI
    AccessioniPrimary (citable) accession number: P0AE12
    Secondary accession number(s): P15272, P78074
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: May 27, 2015
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    AMP nucleosidase binds AMP at the catalytic site, Mg-ATP at an allosteric regulatory site, and inorganic phosphate also at a regulatory site.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.