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Protein

AMP nucleosidase

Gene

amn

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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.

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10039. amn.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000645861 – 484AMP nucleosidaseAdd BLAST484

    Proteomic databases

    PaxDbiP0AE12.
    PRIDEiP0AE12.

    Expressioni

    Inductioni

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

    Interactioni

    Subunit structurei

    Homohexamer. Trimer of dimers.1 Publication

    Protein-protein interaction databases

    BioGridi4260401. 9 interactors.
    IntActiP0AE12. 8 interactors.
    STRINGi511145.b1982.

    Structurei

    Secondary structure

    1484
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 38Combined sources29
    Helixi44 – 47Combined sources4
    Turni48 – 50Combined sources3
    Beta strandi51 – 61Combined sources11
    Beta strandi73 – 75Combined sources3
    Beta strandi78 – 86Combined sources9
    Turni90 – 93Combined sources4
    Helixi94 – 108Combined sources15
    Beta strandi111 – 120Combined sources10
    Helixi123 – 126Combined sources4
    Helixi136 – 145Combined sources10
    Beta strandi169 – 174Combined sources6
    Helixi176 – 190Combined sources15
    Helixi194 – 196Combined sources3
    Beta strandi199 – 205Combined sources7
    Helixi208 – 222Combined sources15
    Beta strandi226 – 233Combined sources8
    Beta strandi238 – 240Combined sources3
    Helixi246 – 248Combined sources3
    Helixi254 – 257Combined sources4
    Beta strandi262 – 267Combined sources6
    Beta strandi273 – 277Combined sources5
    Helixi282 – 292Combined sources11
    Helixi293 – 295Combined sources3
    Beta strandi298 – 302Combined sources5
    Beta strandi305 – 308Combined sources4
    Beta strandi318 – 327Combined sources10
    Turni330 – 334Combined sources5
    Helixi345 – 358Combined sources14
    Helixi363 – 368Combined sources6
    Beta strandi370 – 379Combined sources10
    Helixi383 – 386Combined sources4
    Helixi387 – 397Combined sources11
    Beta strandi399 – 405Combined sources7
    Helixi406 – 415Combined sources10
    Beta strandi420 – 428Combined sources9
    Helixi430 – 432Combined sources3
    Helixi443 – 446Combined sources4
    Helixi448 – 465Combined sources18
    Turni466 – 470Combined sources5
    Helixi473 – 475Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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

    eggNOGiENOG4105FYV. Bacteria.
    COG0775. LUCA.
    HOGENOMiHOG000156781.
    InParanoidiP0AE12.
    KOiK01241.
    OMAiCYPFVRV.
    PhylomeDBiP0AE12.

    Family and domain databases

    Gene3Di3.30.1730.10. 1 hit.
    3.40.50.1580. 1 hit.
    HAMAPiMF_01932. AMP_nucleosidase. 1 hit.
    InterProiIPR011271. AMP_nucleosidase.
    IPR018953. AMP_nucleoside_Pase_N.
    IPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 2 hits.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti300 – 302WLM → CY in AAA23433 (PubMed:2690948).Curated3
    Sequence conflicti311 – 316ESQAIG → KVRPLA in AAA23433 (PubMed:2690948).Curated6

    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.
    WP_001060244.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75046; AAC75046; b1982.
    BAA15802; BAA15802; BAA15802.
    GeneIDi946508.
    KEGGiecj:JW1963.
    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.
    WP_001060244.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260401. 9 interactors.
    IntActiP0AE12. 8 interactors.
    STRINGi511145.b1982.

    Proteomic databases

    PaxDbiP0AE12.
    PRIDEiP0AE12.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75046; AAC75046; b1982.
    BAA15802; BAA15802; BAA15802.
    GeneIDi946508.
    KEGGiecj:JW1963.
    eco:b1982.
    PATRICi32119295. VBIEscCol129921_2060.

    Organism-specific databases

    EchoBASEiEB0037.
    EcoGeneiEG10039. amn.

    Phylogenomic databases

    eggNOGiENOG4105FYV. Bacteria.
    COG0775. LUCA.
    HOGENOMiHOG000156781.
    InParanoidiP0AE12.
    KOiK01241.
    OMAiCYPFVRV.
    PhylomeDBiP0AE12.

    Enzyme and pathway databases

    BioCyciEcoCyc:AMP-NUCLEOSID-MONOMER.
    ECOL316407:JW1963-MONOMER.
    MetaCyc:AMP-NUCLEOSID-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP0AE12.
    PROiP0AE12.

    Family and domain databases

    Gene3Di3.30.1730.10. 1 hit.
    3.40.50.1580. 1 hit.
    HAMAPiMF_01932. AMP_nucleosidase. 1 hit.
    InterProiIPR011271. AMP_nucleosidase.
    IPR018953. AMP_nucleoside_Pase_N.
    IPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 2 hits.
    PfamiPF10423. AMNp_N. 1 hit.
    PF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01717. AMP-nucleosdse. 1 hit.
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 89 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

    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.