P69503 (APT_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Adenine phosphoribosyltransferase Short name=APRT EC=2.4.2.7 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 183 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. HAMAP-Rule MF_00004 |
| Catalytic activity | AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00004 |
| Pathway | Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. HAMAP-Rule MF_00004 |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Sequence similarities | Belongs to the purine/pyrimidine phosphoribosyltransferase family. |
| Sequence caution | The sequence AAB40223.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine salvage |
| Cellular component | Cytoplasm |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | AMP salvage Inferred from electronic annotation. Source: UniProtKB-UniPathway adenine salvageInferred from direct assay PubMed 4328693. Source: EcoCyc purine ribonucleoside salvageInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB |
| Molecular_function | adenine phosphoribosyltransferase activity Inferred from direct assay PubMed 4328693. Source: EcoCyc identical protein bindingInferred from direct assay PubMed 4328693. Source: EcoCyc magnesium ion bindingInferred from direct assay PubMed 4328693. Source: EcoCyc |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 183 | 183 | Adenine phosphoribosyltransferase HAMAP-Rule MF_00004 | PRO_0000149379 | ||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 5 – 14 | 10 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 15 – 18 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 28 – 30 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 32 – 36 | 5 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 38 – 52 | 15 | ||||||||||||||||||||||||||||||||||||||||
| Turn | 53 – 56 | 4 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 63 | 5 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 66 – 78 | 13 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 81 – 87 | 7 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 95 – 102 | 8 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 112 | 8 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 113 – 115 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 121 – 131 | 11 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 133 – 144 | 12 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 148 – 158 | 11 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 159 – 161 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 168 | 6 | ||||||||||||||||||||||||||||||||||||||||
| Turn | 169 – 171 | 3 | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 173 – 180 | 8 | ||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence and deduced amino acid sequence of Escherichia coli adenine phosphoribosyltransferase and comparison with other analogous enzymes." Hershey H.V., Taylor M.W. Gene 43:287-293(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [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 277:1453-1474(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] | "Oligoribonuclease is encoded by a highly conserved gene in the 3'-5' exonuclease superfamily." Zhang X., Zhu L., Deutscher M.P. J. Bacteriol. 180:2779-2781(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7. |
| [6] | "The adjacent dnaZ and dnaX genes of Escherichia coli are contained within one continuous open reading frame." Flower A.M., McHenry C.S. Nucleic Acids Res. 14:8091-8101(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-183. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M14040 Genomic DNA. Translation: AAA23455.1. X04487 Genomic DNA. Translation: CAA28173.1. U82664 Genomic DNA. Translation: AAB40223.1. Different initiation. U00096 Genomic DNA. Translation: AAC73571.1. AP009048 Genomic DNA. Translation: BAE76248.1. M38777 Genomic DNA. Translation: AAA23456.1. | ||||||||||||
| PIR | RTECA. A25635. | ||||||||||||
| RefSeq | NP_415002.1. NC_000913.2. YP_488760.1. NC_007779.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P69503. | ||||||||||||
| SMR | P69503. Positions 2-183. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP-36165N. | ||||||||||||
| IntAct | P69503. 5 interactions. | ||||||||||||
| STRING | 511145.b0469. | ||||||||||||
2D gel databases | |||||||||||||
| SWISS-2DPAGE | P69503. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | P69503. | ||||||||||||
| PRIDE | P69503. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | AAC73571; AAC73571; b0469. BAE76248; BAE76248; BAE76248. | ||||||||||||
| GeneID | 12932353. 945113. | ||||||||||||
| KEGG | ecj:Y75_p0456. eco:b0469. | ||||||||||||
| PATRIC | 32116095. VBIEscCol129921_0489. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0049. | ||||||||||||
| EcoGene | EG10051. apt. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0503. | ||||||||||||
| HOGENOM | HOG000036776. | ||||||||||||
| KO | K00759. | ||||||||||||
| OMA | DYALEYG. | ||||||||||||
| ProtClustDB | PRK02304. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:ADENPRIBOSYLTRAN-MONOMER. ECOL316407:JW0458-MONOMER. MetaCyc:ADENPRIBOSYLTRAN-MONOMER. | ||||||||||||
| UniPathway | UPA00588; UER00646. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P69503. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00004. Aden_phosphoribosyltr. | ||||||||||||
| InterPro | IPR005764. Ade_phspho_trans. IPR000836. PRibTrfase_dom. [Graphical view] | ||||||||||||
| Pfam | PF00156. Pribosyltran. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR01090. apt. 1 hit. | ||||||||||||
| PROSITE | PS00103. PUR_PYR_PR_TRANSFER. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P69503. | ||||||||||||
Entry information
| Entry name | APT_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P69503 Secondary accession number(s): P07672 Q2MBV8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
