KEGG   ENZYME: 2.4.2.54Help
Entry
EC 2.4.2.54                 Enzyme                                 

Name
beta-ribofuranosylphenol 5'-phosphate synthase;
beta-RFAP synthase (incorrect);
beta-RFA-P synthase (incorrect);
AF2089 (gene name);
MJ1427 (gene name);
beta-ribofuranosylhydroxybenzene 5'-phosphate synthase;
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase (incorrect);
beta-ribofuranosylaminobenzene 5'-phosphate synthase (incorrect);
5-phospho-alpha-D-ribose 1-diphosphate:4-aminobenzoate 5-phospho-beta-D-ribofuranosyltransferase (decarboxylating) (incorrect)
Class
Transferases;
Glycosyltransferases;
Pentosyltransferases
BRITE hierarchy
Sysname
5-phospho-alpha-D-ribose-1-diphosphate:4-hydroxybenzoate 5-phospho-beta-D-ribofuranosyltransferase (decarboxylating)
Reaction(IUBMB)
5-phospho-alpha-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate [RN:R11102]
Reaction(KEGG)
R11102;
(other) R10337
Show
Substrate
5-phospho-alpha-D-ribose 1-diphosphate [CPD:C00119];
4-hydroxybenzoate [CPD:C00156]
Product
4-(beta-D-ribofuranosyl)phenol 5'-phosphate [CPD:C21107];
CO2 [CPD:C00011];
diphosphate [CPD:C00013]
Comment
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It was initially thought to use 4-aminobenzoate as a substrate, but was later shown to utilize 4-hydroxybenzoate [4]. The activity is dependent on Mg2+ or Mn2+ [1].
History
EC 2.4.2.54 created 2013, modified 2014, modified 2015
Pathway
ec00790  Folate biosynthesis
Orthology
K06984  beta-ribofuranosylaminobenzene 5'-phosphate synthase
Genes
SBJ: CF168_02950
PSEO: OM33_01310
MMT: Metme_1363
MDH: AYM39_07270
AFA: UZ73_08470
SULR: B649_07545
NTP: CRH09_08300
SAQ: Sare_0579
MJA: MJ_1427
MFE: Mefer_1394
MMP: MMP0279(mptG)
MMD: GYY_01430
MAE: Maeo_0244
MVO: Mvol_1337
MBU: Mbur_1563
MMET: MCMEM_2074
MMH: Mmah_0135
MPY: Mpsy_1935
MTP: Mthe_0935
MCJ: MCON_2372
MHI: Mhar_2046
MHU: Mhun_1148
MEMA: MMAB1_2341
MPI: Mpet_2520
MPL: Mpal_1624
MPD: MCP_1555(mptG-1) MCP_1942(mptG-2)
MEZ: Mtc_1505
MTH: MTH_830
METC: MTCT_0744
METE: tca_00797(thrB_2)
MRU: mru_1690(mptG)
MEB: Abm4_0511(mptG1) Abm4_0513(mptG2)
MMIL: sm9_1728(mptG1) sm9_1774(mptG2)
MEYE: TL18_04245
MOL: YLM1_1158
METH: MBMB1_0695
MFC: BRM9_1500(mptG)
MCUB: MCBB_0706
MFV: Mfer_0206
MKA: MK0558
AFU: AF_2089
FPL: Ferp_2137
GAC: GACE_1235
GAH: GAH_01805
HHB: Hhub_3126
HMA: rrnAC0303(ghmP)
HHI: HAH_1044(ghmP)
NPH: NP_4930A
NMO: Nmlp_3439
HUT: Huta_2356
HTI: HTIA_1898
HMU: Hmuk_1348
HWA: HQ_3191A
HWC: Hqrw_3752
HVO: HVO_2628
HME: HFX_2645
HTU: Htur_2109
NMG: Nmag_0626
NAT: NJ7G_1238
SALI: L593_05040
PHO: PH0227(PH0227) PH1228(PH1228)
PFU: PF0903
PFI: PFC_03735
TON: TON_0388
TGA: TGAM_1652(ghmP)
TSI: TSIB_0667
THE: GQS_03285
THM: CL1_0331
TLT: OCC_00267
THS: TES1_0523
TEU: TEU_07325
PPAC: PAP_03835
IHO: Igni_1441
IIS: EYM_04885
TAG: Tagg_0600
HBU: Hbut_0952
SSO: SSO0370
SOL: Ssol_1345
SSOA: SULA_1388
SSOL: SULB_1389
SSOF: SULC_1387
STO: STK_13890
SAI: Saci_1486
SID: M164_1780
SII: LD85_1990
SIH: SiH_1709
SIR: SiRe_1629
SIC: SiL_1622
MSE: Msed_1616
MCN: Mcup_0611
AHO: Ahos_1268
 » show all
Taxonomy
Reference
1  [PMID:9698382]
  Authors
Rasche ME, White RH
  Title
Mechanism for the enzymatic formation of 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate during the biosynthesis of methanopterin.
  Journal
Biochemistry 37:11343-51 (1998)
DOI:10.1021/bi973086q
Reference
2  [PMID:12142414]
  Authors
Scott JW, Rasche ME
  Title
Purification, overproduction, and partial characterization of beta-RFAP synthase, a key enzyme in the methanopterin biosynthesis pathway.
  Journal
J Bacteriol 184:4442-8 (2002)
DOI:10.1128/JB.184.16.4442-4448.2002
  Sequence
[afu:AF_2089]
Reference
3  [PMID:15262968]
  Authors
Dumitru RV, Ragsdale SW
  Title
Mechanism of 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase, a key enzyme in the methanopterin biosynthetic pathway.
  Journal
J Biol Chem 279:39389-95 (2004)
DOI:10.1074/jbc.M406442200
  Sequence
[mja:MJ_1427]
Reference
4  [PMID:21634403]
  Authors
White RH
  Title
The conversion of a phenol to an aniline occurs in the biochemical formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in methanopterin.
  Journal
Biochemistry 50:6041-52 (2011)
DOI:10.1021/bi200362w
Other DBs
ExplorEnz - The Enzyme Database: 2.4.2.54
IUBMB Enzyme Nomenclature: 2.4.2.54
ExPASy - ENZYME nomenclature database: 2.4.2.54
BRENDA, the Enzyme Database: 2.4.2.54

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