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Protein

AMP nucleosidase

Gene

amn

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

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

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

    Keywordsi

    Molecular functionAllosteric enzyme, Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:AMP-NUCLEOSID-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

    Pathology & Biotechi

    Disruption phenotypei

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

    Chemistry databases

    DrugBankiDB03464 Formycin-5'-Monophosphate

    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, 10 interactors
    IntActiP0AE12, 8 interactors
    STRINGi316385.ECDH10B_2126

    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
    OMAiRPHAWIM
    PhylomeDBiP0AE12

    Family and domain databases

    Gene3Di3.30.1730.10, 1 hit
    HAMAPiMF_01932 AMP_nucleosidase, 1 hit
    InterProiView protein in InterPro
    IPR037109 AMP_N_sf
    IPR011271 AMP_nucleosidase
    IPR018953 AMP_nucleoside_Pase_N
    IPR000845 Nucleoside_phosphorylase_d
    IPR035994 Nucleoside_phosphorylase_sf
    PANTHERiPTHR43691:SF6 PTHR43691:SF6, 1 hit
    PfamiView protein in Pfam
    PF10423 AMNp_N, 1 hit
    PF01048 PNP_UDP_1, 1 hit
    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
    PATRICifig|1411691.4.peg.269

    Similar proteinsi

    Entry informationi

    Entry nameiAMN_ECOLI
    AccessioniPrimary (citable) accession number: P0AE12
    Secondary accession number(s): P15272, P78074
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: March 28, 2018
    This is version 97 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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

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