RFHPS_ARCFU
ID RFHPS_ARCFU Reviewed; 313 AA.
AC O28190;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Beta-ribofuranosylphenol 5'-phosphate synthase {ECO:0000305};
DE EC=2.4.2.54 {ECO:0000250|UniProtKB:Q58822};
DE AltName: Full=Beta-ribofuranosylaminobenzene 5'-phosphate synthase {ECO:0000305};
DE Short=Beta-RFA-P synthase {ECO:0000303|PubMed:12142414};
DE AltName: Full=Beta-ribofuranosylhydroxybenzene 5'-phosphate synthase {ECO:0000305};
DE Short=Beta-RFH-P synthase {ECO:0000305};
GN OrderedLocusNames=AF_2089;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RX PubMed=12142414; DOI=10.1128/jb.184.16.4442-4448.2002;
RA Scott J.W., Rasche M.E.;
RT "Purification, overproduction, and partial characterization of beta-RFAP
RT synthase, a key enzyme in the methanopterin biosynthesis pathway.";
RL J. Bacteriol. 184:4442-4448(2002).
CC -!- FUNCTION: Catalyzes the condensation of 4-hydroxybenzoate (HB) with 5-
CC phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-
CC ribofuranosylphenol 5'-phosphate (beta-RFH-P) (By similarity). Also
CC catalyzes the condensation of 4-aminobenzoate (pABA) with PRPP to
CC produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P)
CC (PubMed:12142414). {ECO:0000250|UniProtKB:Q58822,
CC ECO:0000269|PubMed:12142414}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + 5-phospho-alpha-D-ribose 1-diphosphate +
CC H(+) = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 +
CC diphosphate; Xref=Rhea:RHEA:48556, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:82767; EC=2.4.2.54;
CC Evidence={ECO:0000250|UniProtKB:Q58822};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48557;
CC Evidence={ECO:0000250|UniProtKB:Q58822};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobenzoate + 5-phospho-alpha-D-ribose 1-diphosphate +
CC H(+) = 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 +
CC diphosphate; Xref=Rhea:RHEA:35815, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17836, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:72778;
CC Evidence={ECO:0000269|PubMed:12142414};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35816;
CC Evidence={ECO:0000269|PubMed:12142414};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3. {ECO:0000269|PubMed:12142414};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:12142414};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000305|PubMed:12142414}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12142414}.
CC -!- SIMILARITY: Belongs to the beta-RFA-P synthase family. {ECO:0000305}.
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DR EMBL; AE000782; AAB89167.1; -; Genomic_DNA.
DR PIR; H69510; H69510.
DR RefSeq; WP_010879581.1; NC_000917.1.
DR AlphaFoldDB; O28190; -.
DR SMR; O28190; -.
DR STRING; 224325.AF_2089; -.
DR EnsemblBacteria; AAB89167; AAB89167; AF_2089.
DR GeneID; 24795837; -.
DR KEGG; afu:AF_2089; -.
DR eggNOG; arCOG01026; Archaea.
DR HOGENOM; CLU_061764_0_0_2; -.
DR OMA; RLNGAWY; -.
DR OrthoDB; 47243at2157; -.
DR PhylomeDB; O28190; -.
DR BRENDA; 2.4.2.54; 414.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR004422; RFAP_synthase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR20861:SF6; PTHR20861:SF6; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF004884; Sugar_kin_arch; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00144; beta_RFAP_syn; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="Beta-ribofuranosylphenol 5'-phosphate synthase"
FT /id="PRO_0000107322"
SQ SEQUENCE 313 AA; 34075 MW; BFF87594559030CA CRC64;
MLRLRTPSRI HITLIDLNGS IGRVDGGVGL ALEEPHIEIK AKESETFVLK GEPINRERFE
IAAAKMAEYC GRGAEIEVVS DYDAHVGLGS GTQISLAVGR AFSELYGLNL TTRQIAEIMG
RGGTSGIGVA VFDHGGLVVD GGHSTKEKKS FLPSSASRAK PAPMIARLDF PDWNVVLAIP
DLKGFFGERE VNLFQKSCPV PLEDVREICH LILMKMLPAV VEADLDEFGK ALKRIQELGF
KKAEVEQYGE LIKGCFDLAD CIGMSSTGPT VYAITDSNAG GIERSLRDYF AEKGYECRTI
VTKARNRGVE IEV
