| Entry |
|
| Name |
ribose 1,5-bisphosphate phosphokinase;
ribose 1,5-bisphosphokinase;
PhnN;
ATP:ribose-1,5-bisphosphate phosphotransferase
|
| Class |
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with a phosphate group as acceptor
 |
| Sysname |
ATP:alpha-D-ribose-1,5-bisphosphate phosphotransferase
|
| Reaction(IUBMB) |
ATP + alpha-D-ribose 1,5-bisphosphate = ADP + 5-phospho-alpha-D-ribose 1-diphosphate [RN: R06836]
|
| Reaction(KEGG) |
|
| Substrate |
ATP [CPD: C00002];
alpha-D-ribose 1,5-bisphosphate [CPD: C01151]
|
| Product |
ADP [CPD: C00008];
5-phospho-alpha-D-ribose 1-diphosphate [CPD: C00119]
|
| Comment |
This enzyme, found in NAD supression mutants of Escherichia coli, synthesizes 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) without the participation of EC 2.7.6.1, ribose-phosphate diphosphokinase. Ribose, ribose 1-phosphate and ribose 5-phosphate are not substrates, and GTP cannot act as a phosphate donor.
|
| Pathway |
| Pentose phosphate pathway |
|
| Orthology |
| ribose 1,5-bisphosphokinase |
|
| Genes |
ECO: | | ECJ: | | ECD: | | EBW: | | ECOK: | | ECE: | | ECS: | | ECF: | | ETW: | | ELX: | | EOJ: | | EOI: | | EOH: | | ECG: | | EOK: | | ELR: | | ECP: | | ECI: | | ECV: | | ECX: | | ECW: | | ECM: | | ECY: | | ECR: | | ECQ: | | ECK: | | ECT: | | EOC: | | EUM: | | ECZ: | | ELO: | | ELN: | | ELH: | | ESE: | | ESO: | | ESM: | | ESL: | | ECL: | | EBR: | | EBD: | | EKO: | | EKF: | | EAB: | | EDH: | | EDJ: | | EIH: | | ENA: | | ELU: | | EUN: | | ELW: | | ELL: | | ELC: | | ELD: | | ELP: | | EBL: | | EBE: | | ELF: | | ECOA: | | SES: | | YPE: | | YPK: | | YPA: | | YPN: | | YPM: | | YPP: | | YPG: | | YPZ: | | YPT: | | YPD: | | YPX: | | YPH: | | YPS: | | YPI: | | YPY: | | YPB: | | YEN: | | YEP: | | YEY: | | SSN: | | SSJ: | | SBO: | | SDY: | | ECA: | | PCT: | | PCC: | | PWA: | | PEC: | | EBI: | | ENT: | | ENC: | | ENO: | | ECLO: | | ESC: | | EEC: | | ENL: | | EAS: | | EAE: | | EAR: | | KPN: | | KPU: | | KPM: | | KPP: | | KPE: | | KPO: | | KVA: | | KOX: | | CKO: | | SPE: | | SRR: | | SRS: | | SRA: | | SMAF: | | SMW: | | DDA: | | DDC: | | DDD: | | DZE: | | PAM: | | PLF: | | PAJ: | | PAQ: | | PVA: | | PAO: | | RAH: | | RAQ: | | RAA: | | ROR: | | EBF: | | PAE: | | PAU: | | PAP: | | PAG: | | PAF: | | PNC: | | PDK: | | PSG: | | PPU: | | PPF: | | PPG: | | PPW: | | PPT: | | PPB: | | PPI: | | PPX: | | PPUH: | | PPUU: | | PST: | | PSB: | | PSP: | | PFO: | | PFS: | | PFC: | | PPZ: | | PEN: | | PMY: | | PMK: | | PSA: | | PSZ: | | PSR: | | PSC: | | PSJ: | | PSH: | | PFV: | | PDR: | | AVN: | | AVL: | | AVD: | | SWD: | | MAQ: | | MBS: | | PIN: | | TCX: | | AFE: | | AFR: | | CVI: | | LHK: | | REU: | | REH: | | RME: | | CTI: | | CNC: | | BMA: | | BMV: | | BML: | | BMN: | | BPS: | | BPM: | | BPL: | | BPD: | | BPR: | | BPZ: | | BPQ: | | BTD: | | BXE: | | BPH: | | BPY: | | BUG: | | BGE: | | BGF: | | BYI: | | BPX: | | AXY: | | PUT: | | AKA: | | RFR: | | DIA: | | ACK: | | VEI: | | VAP: | | RTA: | | MPT: | | TBD: | | GCA: | | ANT: | | DDE: | | DDN: | | DAS: | | DPI: | | DBA: | | DSF: | | MLO: | | MCI: | | MOP: | | MAM: | | MES: | | SME: | | SMK: | | SMQ: | | SMX: | | SMI: | | SMEG: | | SMEL: | | SMD: | | RHI: | | SFH: | | SFD: | | ATU: | | ARA: | | AVI: | | AGR: | | RET: | | REC: | | RLE: | | RLT: | | RLG: | | RTR: | | BME: | | BMI: | | BMZ: | | BMG: | | BMW: | | BMF: | | BMB: | | BMC: | | BAA: | | BMS: | | BSI: | | BMT: | | BSV: | | BOV: | | BCS: | | BSK: | | BMR: | | BPP: | | OAN: | | BJA: | | BJU: | | BRA: | | BBT: | | BRS: | | RPA: | | RPB: | | RPC: | | RPD: | | RPE: | | RPT: | | RPX: | | AOL: | | XAU: | | AZC: | | SNO: | | MRD: | | MET: | | MNO: | | SIL: | | SIT: | | RCP: | | JAN: | | RDE: | | RLI: | | PDE: | | PSF: | | PGA: | | PGL: | | OAT: | | OAR: | | ACR: | | AMV: | | TMO: | | PGV: | | CMI: | | FRI: | | PLP: | | » show all
 |
| Reference |
|
| Authors |
Hove-Jensen B, Rosenkrantz TJ, Haldimann A, Wanner BL. |
| Title |
Escherichia coli phnN, encoding ribose 1,5-bisphosphokinase activity (phosphoribosyl diphosphate forming): dual role in phosphonate degradation and NAD biosynthesis pathways. |
| Journal |
J. Bacteriol. 185 (2003) 2793-801. |
| Organism |
Escherichia coli [GN: eco] |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |