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P0AE12

- AMN_ECOLI

UniProt

P0AE12 - AMN_ECOLI

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Protein
AMP nucleosidase
Gene
amn, b1982, JW1963
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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
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.
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 nucleosidase
PRO_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

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3023WLM → CY in AAA23433. 1 Publication
Sequence conflicti311 – 3166ESQAIG → KVRPLA in AAA23433. 1 Publication

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

« 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.
  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: July 9, 2014
This is version 76 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

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