KEGG   ENZYME: 2.4.2.57
Entry
EC 2.4.2.57                 Enzyme                                 
Name
AMP phosphorylase;
AMPpase;
nucleoside monophosphate phosphorylase;
deoA (gene name)
Class
Transferases;
Glycosyltransferases;
Pentosyltransferases
Sysname
AMP:phosphate alpha-D-ribosyl 5'-phosphate-transferase
Reaction(IUBMB)
(1) AMP + phosphate = adenine + alpha-D-ribose 1,5-bisphosphate [RN:R10836];
(2) CMP + phosphate = cytosine + alpha-D-ribose 1,5-bisphosphate [RN:R10837];
(3) UMP + phosphate = uracil + alpha-D-ribose 1,5-bisphosphate [RN:R10838]
Reaction(KEGG)
Substrate
AMP [CPD:C00020];
phosphate [CPD:C00009];
CMP [CPD:C00055];
UMP [CPD:C00105]
Product
adenine [CPD:C00147];
alpha-D-ribose 1,5-bisphosphate [CPD:C01151];
cytosine [CPD:C00380];
uracil [CPD:C00106]
Comment
The enzyme from archaea is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The activity with CMP and UMP requires activation by cAMP [2].
History
EC 2.4.2.57 created 2014
Pathway
ec00230  Purine metabolism
ec00240  Pyrimidine metabolism
ec01100  Metabolic pathways
Orthology
K18931  AMP phosphorylase
Genes
SRBP148_SR1C001G0223
MJAMJ_0667
MFEMefer_1403
MVUMetvu_0291
MFSMFS40622_1516
MIFMetin_0751
MJHJH146_1232
MESGMLAUSG7_0441
MESAMLASG1_0067
MIGMetig_0832
MMPMMP0327(deoA)
MMQMmarC5_1346
MMXMmarC6_0624
MMZMmarC7_1329
MMDGYY_01685
MMAKMMKA1_03350(deoA)
MMAOMMOS7_03620(deoA)
MMADMMJJ_07310(pdp)
MAEMaeo_0618
MVNMevan_1338
MVOMvol_1718
MOKMetok_1244
METFCFE53_03450
AFUAF_1341 AF_1342
AFGAFULGI_00014530 AFULGI_00014540
APOArcpr_1123
AVEArcve_0240 Arcve_2095
ASTAsulf_01770 Asulf_01771
FPLFerp_0811
GACGACE_0123
GAHGAH_00259
PFUPF1607
PFIPFC_10580
PHOPH1598(PH1598)
PABPAB1982
PYNPNA2_0183
PYAPYCH_04830
PYSPy04_1485
PYCTQ32_08875
TKOTK0352
TONTON_1062
TGATGAM_1786
TSITSIB_0680
TBATERMP_01023
THEGQS_10255
THATAM4_270
THMCL1_1626
TLTOCC_02747
THSTES1_1098
TNUBD01_1010
TEUTEU_10940
TGYX802_02315
THVADU37_CDS06780
TCHCHITON_1834
TPEPA0127_02550
TPIEA7C91_00800
TGGA3K92_01245
TCEA3L02_05060
TBSA3L01_06040
THHCDI07_05995
TSLA3L11_10085
TTDA3L14_08440
TPRFA3L09_03120
TRLA3L10_00560
TPAFA3L08_09185
THYA3L12_06725
TICFH039_07700
TCQTIRI35C_1520
THEMFPV09_01725
THEIK1720_06545
PPACPAP_04670
MBAMbar_A3188
MBYMSBRM_2287
MBWMSBRW_1549
MBARMSBR2_0125
MBAKMSBR3_0180
MACMA_3242(deoA)
MMAMM_0087
MMAZMmTuc01_0096
MMJMSMAS_1243
MMACMSMAC_2591
MVCMSVAZ_1622
MEKMSKOL_1551
MLSMSLAZ_1586
METMMSMTP_1230
MEFMSWH1_2026
MEQMSWHS_3043
MSJMSSAC_1182
MSZMSSIH_2777
MSWMSSIT_2809
MTHRMSTHT_0154
MTHEMSTHC_0574
MHORMSHOH_2091
MFZAOB57_001685
MBUMbur_0255
MMETMCMEM_0874
MELOJ7W08_02610
MMHMmah_1278
MHAZBHR79_07150
MPOTBKM01_03400
MEVMetev_0684
MZHMzhil_0675
MPYMpsy_0111
MZIHWN40_05870
MMAVRE476_02540
MSEBRE474_12380
MHZMetho_1154
MTPMthe_0462
MCJMCON_0583
MHIMhar_0827 Mhar_1625
MHUMhun_2262
MRTJKHC33_15725
MLAMlab_0067
MEMMemar_0551
MBGBN140_1665(deoA)
MEMAMMAB1_2139
MCHKMchiMG62_06790
MSUMOH143_09480
MRCR6Y96_00015
MPIMpet_0506
MENDL6E24_05320
MEFWF1737_08660
MAQERJ40_06415
MFKE2N92_06550
MOUOU421_03255
MESBL1S32_06860
MANQL1994_08825
MBNMboo_0523
MFOMetfor_2665
MPLMpal_2125
MPDMCP_0060
MEZMtc_0258(deoA)
RCIRCIX1126(deoA)
HARAAArcS_1364(deoA)
NPHNP_3958A(deoA)
HALIBV210_04495
SSAIN0B31_08630
HVOHVO_0965(deoA)
HMEHFX_0962(deoA)
HGIABY42_04630
HALEG3A49_04810
HLSKU306_09415
HLNSVXHx_0918(ampp)
HBOHbor_21600
HLMDV707_15785
SRUBC2R22_06165
HDFAArcSl_0205(deoA)
NMGNmag_4015(deoA)
NAJB1756_15370
NAGAArcMg_2615
NANAArc1_1083
NARAQQ977_06435
NBGDV706_02185
NASGCU68_11445
MEAMMU439_00575
MEAEQEN48_02095
TARTALC_00201
MAXMMALV_01880
MERMMINT_17690
MEARMpt1_c12740
MEUZKRP56_01055
MARCAR505_0705 AR505_1641
ABIAboo_0332
ACFAciM339_0725
SHCShell_0989
DKADKAM_0158
DFDDesfe_0233
DMUDesmu_0291
TAGTagg_0379
THGTCELL_1247
HBUHbut_0381
PDLPyrde_2037
PABIPABY_20650
PAREPYJP_20540
TPETpen_0093
THBN186_01385
TCBTCARB_1361
THELIG193_07085
NUEC5F50_03375
NIUDSQ19_01120
NCKQVH35_04710
BARCAOA65_1927
FLTSv326_0528
LOBNEF87_004614 NEF87_004615
PSYTDSAG12_02244
AGWQT03_C0001G0516
 » show all
Reference
1  [PMID:17303759]
  Authors
Sato T, Atomi H, Imanaka T
  Title
Archaeal type III RuBisCOs function in a pathway for AMP metabolism.
  Journal
Science 315:1003-6 (2007)
DOI:10.1126/science.1135999
  Sequence
[tko:TK0352]
Reference
2  [PMID:23065974]
  Authors
Aono R, Sato T, Yano A, Yoshida S, Nishitani Y, Miki K, Imanaka T, Atomi H
  Title
Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway.
  Journal
J Bacteriol 194:6847-55 (2012)
DOI:10.1128/JB.01335-12
  Sequence
[tko:TK0352]
Reference
3  [PMID:23659790]
  Authors
Nishitani Y, Aono R, Nakamura A, Sato T, Atomi H, Imanaka T, Miki K
  Title
Structure analysis of archaeal AMP phosphorylase reveals two unique modes of dimerization.
  Journal
J Mol Biol 425:2709-21 (2013)
DOI:10.1016/j.jmb.2013.04.026
  Sequence
[tko:TK0352]
Other DBs
ExplorEnz - The Enzyme Database: 2.4.2.57
IUBMB Enzyme Nomenclature: 2.4.2.57
ExPASy - ENZYME nomenclature database: 2.4.2.57
BRENDA, the Enzyme Database: 2.4.2.57

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