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P0AE12 (AMN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AMP nucleosidase

EC=3.2.2.4
Gene names
Name:amn
Ordered Locus Names:b1982, JW1963
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in regulation of AMP concentrations.

Catalytic activity

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

Enzyme regulation

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

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.

Induction

By cAMP at limiting phosphate concentrations. Repressed by phosphate.

Miscellaneous

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

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processAMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionAMP nucleosidase activity

Inferred from direct assay PubMed 7000783. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484AMP nucleosidase
PRO_0000064586

Experimental info

Sequence conflict300 – 3023WLM → CY in AAA23433. Ref.1
Sequence conflict311 – 3166ESQAIG → KVRPLA in AAA23433. Ref.1

Secondary structure

............................................................................ 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AE12 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: ADC2FD95CC220527

FASTA48453,995
        10         20         30         40         50         60 
MNNKGSGLTP AQALDKLDAL YEQSVVALRN AIGNYITSGE LPDENARKQG LFVYPSLTVT 

        70         80         90        100        110        120 
WDGSTTNPPK TRAFGRFTHA GSYTTTITRP TLFRSYLNEQ LTLLYQDYGA HISVQPSQHE 

       130        140        150        160        170        180 
IPYPYVIDGS ELTLDRSMSA GLTRYFPTTE LAQIGDETAD GIYHPTEFSP LSHFDARRVD 

       190        200        210        220        230        240 
FSLARLRHYT GTPVEHFQPF VLFTNYTRYV DEFVRWGCSQ ILDPDSPYIA LSCAGGNWIT 

       250        260        270        280        290        300 
AETEAPEEAI SDLAWKKHQM PAWHLITADG QGITLVNIGV GPSNAKTICD HLAVLRPDVW 

       310        320        330        340        350        360 
LMIGHCGGLR ESQAIGDYVL AHAYLRDDHV LDAVLPPDIP IPSIAEVQRA LYDATKLVSG 

       370        380        390        400        410        420 
RPGEEVKQRL RTGTVVTTDD RNWELRYSAS ALRFNLSRAV AIDMESATIA AQGYRFRVPY 

       430        440        450        460        470        480 
GTLLCVSDKP LHGEIKLPGQ ANRFYEGAIS EHLQIGIRAI DLLRAEGDRL HSRKLRTFNE 


PPFR 

« Hide

References

« Hide 'large scale' references
[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]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30469 Genomic DNA. Translation: AAA23433.1.
U00096 Genomic DNA. Translation: AAC75046.1.
AP009048 Genomic DNA. Translation: BAA15802.1.
U88529 Genomic DNA. Translation: AAC46272.1.
PIRH64962.
RefSeqNP_416489.1. NC_000913.3.
YP_490228.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0AE12.
SMRP0AE12. Positions 8-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0AE12. 8 interactions.
STRING511145.b1982.

Proteomic databases

PaxDbP0AE12.
PRIDEP0AE12.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75046; AAC75046; b1982.
BAA15802; BAA15802; BAA15802.
GeneID12931407.
946508.
KEGGecj:Y75_p1946.
eco:b1982.
PATRIC32119295. VBIEscCol129921_2060.

Organism-specific databases

EchoBASEEB0037.
EcoGeneEG10039. amn.

Phylogenomic databases

eggNOGCOG0775.
HOGENOMHOG000156781.
KOK01241.
OMAQNIPYPY.
OrthoDBEOG67DPGS.
PhylomeDBP0AE12.

Enzyme and pathway databases

BioCycEcoCyc:AMP-NUCLEOSID-MONOMER.
ECOL316407:JW1963-MONOMER.
MetaCyc:AMP-NUCLEOSID-MONOMER.
RETL1328306-WGS:GSTH-1334-MONOMER.
UniPathwayUPA00588; UER00646.

Gene expression databases

GenevestigatorP0AE12.

Family and domain databases

Gene3D3.30.1730.10. 1 hit.
3.40.50.1580. 1 hit.
InterProIPR011271. AMP_nucleosidase.
IPR018953. AMP_nucleoside_Pase_N.
IPR018017. Nucleoside_phosphorylase.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PfamPF10423. AMNp_N. 1 hit.
PF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01717. AMP-nucleosdse. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0AE12.
PROP0AE12.

Entry information

Entry nameAMN_ECOLI
AccessionPrimary (citable) accession number: P0AE12
Secondary accession number(s): P15272, P78074
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene