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P0AE12

- AMN_ECOLI

UniProt

P0AE12 - AMN_ECOLI

Protein

AMP nucleosidase

Gene

amn

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Involved in regulation of AMP concentrations.

    Catalytic activityi

    AMP + H2O = D-ribose 5-phosphate + adenine.

    Enzyme regulationi

    Allosterically activated by Mg-ATP, and inactivated by inorganic phosphate.

    Pathwayi

    GO - Molecular functioni

    1. AMP nucleosidase activity Source: EcoCyc

    GO - Biological processi

    1. AMP salvage Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:AMP-NUCLEOSID-MONOMER.
    ECOL316407:JW1963-MONOMER.
    MetaCyc:AMP-NUCLEOSID-MONOMER.
    RETL1328306-WGS:GSTH-1334-MONOMER.
    UniPathwayiUPA00588; UER00646.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AMP nucleosidase (EC:3.2.2.4)
    Gene namesi
    Name:amn
    Ordered Locus Names:b1982, JW1963
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10039. amn.

    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.

    Gene expression databases

    GenevestigatoriP0AE12.

    Interactioni

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    Phylogenomic databases

    eggNOGiCOG0775.
    HOGENOMiHOG000156781.
    KOiK01241.
    OMAiQNIPYPY.
    OrthoDBiEOG67DPGS.
    PhylomeDBiP0AE12.

    Family and domain databases

    Gene3Di3.30.1730.10. 1 hit.
    3.40.50.1580. 1 hit.
    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

    MNNKGSGLTP AQALDKLDAL YEQSVVALRN AIGNYITSGE LPDENARKQG    50
    LFVYPSLTVT WDGSTTNPPK TRAFGRFTHA GSYTTTITRP TLFRSYLNEQ 100
    LTLLYQDYGA HISVQPSQHE IPYPYVIDGS ELTLDRSMSA GLTRYFPTTE 150
    LAQIGDETAD GIYHPTEFSP LSHFDARRVD FSLARLRHYT GTPVEHFQPF 200
    VLFTNYTRYV DEFVRWGCSQ ILDPDSPYIA LSCAGGNWIT AETEAPEEAI 250
    SDLAWKKHQM PAWHLITADG QGITLVNIGV GPSNAKTICD HLAVLRPDVW 300
    LMIGHCGGLR ESQAIGDYVL AHAYLRDDHV LDAVLPPDIP IPSIAEVQRA 350
    LYDATKLVSG RPGEEVKQRL RTGTVVTTDD RNWELRYSAS ALRFNLSRAV 400
    AIDMESATIA AQGYRFRVPY GTLLCVSDKP LHGEIKLPGQ ANRFYEGAIS 450
    EHLQIGIRAI DLLRAEGDRL HSRKLRTFNE PPFR 484
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490228.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75046; AAC75046; b1982.
    BAA15802; BAA15802; BAA15802.
    GeneIDi12931407.
    946508.
    KEGGiecj:Y75_p1946.
    eco:b1982.
    PATRICi32119295. VBIEscCol129921_2060.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi H64962.
    RefSeqi NP_416489.1. NC_000913.3.
    YP_490228.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T8R X-ray 2.70 A/B/C/D/E/F 1-484 [» ]
    1T8S X-ray 2.60 A/B/C/D/E/F 1-484 [» ]
    1T8W X-ray 2.80 A/B/C/D/E/F 1-484 [» ]
    1T8Y X-ray 3.00 A/B/C/D/E/F 1-484 [» ]
    ProteinModelPortali P0AE12.
    SMRi P0AE12. Positions 8-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0AE12. 8 interactions.
    STRINGi 511145.b1982.

    Proteomic databases

    PaxDbi P0AE12.
    PRIDEi P0AE12.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75046 ; AAC75046 ; b1982 .
    BAA15802 ; BAA15802 ; BAA15802 .
    GeneIDi 12931407.
    946508.
    KEGGi ecj:Y75_p1946.
    eco:b1982.
    PATRICi 32119295. VBIEscCol129921_2060.

    Organism-specific databases

    EchoBASEi EB0037.
    EcoGenei EG10039. amn.

    Phylogenomic databases

    eggNOGi COG0775.
    HOGENOMi HOG000156781.
    KOi K01241.
    OMAi QNIPYPY.
    OrthoDBi EOG67DPGS.
    PhylomeDBi P0AE12.

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00646 .
    BioCyci EcoCyc:AMP-NUCLEOSID-MONOMER.
    ECOL316407:JW1963-MONOMER.
    MetaCyc:AMP-NUCLEOSID-MONOMER.
    RETL1328306-WGS:GSTH-1334-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AE12.
    PROi P0AE12.

    Gene expression databases

    Genevestigatori P0AE12.

    Family and domain databases

    Gene3Di 3.30.1730.10. 1 hit.
    3.40.50.1580. 1 hit.
    InterProi IPR011271. AMP_nucleosidase.
    IPR018953. AMP_nucleoside_Pase_N.
    IPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view ]
    PANTHERi PTHR21234. PTHR21234. 1 hit.
    Pfami PF10423. AMNp_N. 1 hit.
    PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01717. AMP-nucleosdse. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
    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. "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.

    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: October 1, 2014
    This is version 77 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.

    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3