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P0AE12

- AMN_ECOLI

UniProt

P0AE12 - AMN_ECOLI

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Protein

AMP nucleosidase

Gene

amn

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.1 PublicationUniRule annotation

Catalytic activityi

AMP + H2O = D-ribose 5-phosphate + adenine.1 PublicationUniRule annotation

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

  1. AMP nucleosidase activity Source: EcoCyc

GO - Biological processi

  1. AMP salvage Source: UniProtKB-UniPathway
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:3.2.2.41 PublicationUniRule annotation)
Gene namesi
Name:amn1 PublicationUniRule annotation
Ordered Locus Names:b1982Imported, JW1963Imported
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: 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.CuratedUniRule annotation

Phylogenomic databases

eggNOGiCOG0775.
HOGENOMiHOG000156781.
InParanoidiP0AE12.
KOiK01241.
OMAiQNIPYPY.
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.
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:
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 .
PIRi H64962.
RefSeqi NP_416489.1. NC_000913.3.
YP_490228.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P0AE12.
KOi K01241.
OMAi QNIPYPY.
OrthoDBi EOG67DPGS.
PhylomeDBi P0AE12.

Enzyme and pathway databases

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.
HAMAPi MF_01932. AMP_nucleosidase.
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

« 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: November 26, 2014
This is version 79 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