RFHPS_METTH
ID RFHPS_METTH Reviewed; 329 AA.
AC O26918;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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:0000303|PubMed:31663056};
DE Short=Beta-RFA-P synthase;
DE Short=RFAP synthase {ECO:0000303|PubMed:31663056};
DE AltName: Full=Beta-ribofuranosylhydroxybenzene 5'-phosphate synthase {ECO:0000305};
DE Short=Beta-RFH-P synthase;
GN OrderedLocusNames=MTH_830;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF ASP-19 AND ARG-26.
RX PubMed=31663056; DOI=10.3934/microbiol.2019.3.186;
RA Bechard M.E., Farahani P., Greene D., Pham A., Orry A., Rasche M.E.;
RT "Purification, kinetic characterization, and site-directed mutagenesis of
RT Methanothermobacter thermautotrophicus RFAP Synthase Produced in
RT Escherichia coli.";
RL AIMS Microbiol. 5:186-204(2019).
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:31663056). Only 4-hydroxybenzoate is known to be biosynthesized
CC by methanogenic archaea, but 4-aminobenzoate can be used as substrate
CC by growing methanogens when it is present in the growth medium (By
CC similarity). {ECO:0000250|UniProtKB:Q58822,
CC ECO:0000269|PubMed:31663056}.
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:31663056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35816;
CC Evidence={ECO:0000269|PubMed:31663056};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:31663056};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 mM for pABA (at 70 degrees Celsius);
CC KM=3.9 mM for pABA (at 50 degrees Celsius);
CC Vmax=190 nmol/min/mg enzyme with pABA as substrate (at 70 degrees
CC Celsius);
CC Vmax=1.45 nmol/min/mg enzyme with pABA as substrate (at 50 degrees
CC Celsius);
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:31663056};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:31663056};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000250|UniProtKB:Q58822}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31663056}.
CC -!- SIMILARITY: Belongs to the beta-RFA-P synthase family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85328.1; -; Genomic_DNA.
DR PIR; G69210; G69210.
DR AlphaFoldDB; O26918; -.
DR SMR; O26918; -.
DR STRING; 187420.MTH_830; -.
DR EnsemblBacteria; AAB85328; AAB85328; MTH_830.
DR KEGG; mth:MTH_830; -.
DR PATRIC; fig|187420.15.peg.813; -.
DR HOGENOM; CLU_061764_0_0_2; -.
DR OMA; RLNGAWY; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000005223; 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; Magnesium; Reference proteome; Transferase.
FT CHAIN 1..329
FT /note="Beta-ribofuranosylphenol 5'-phosphate synthase"
FT /id="PRO_0000107321"
FT MUTAGEN 19
FT /note="D->N: 3-fold increase in Km for pABA and 3-fold
FT decrease in Vmax."
FT /evidence="ECO:0000269|PubMed:31663056"
FT MUTAGEN 26
FT /note="R->K: 10-fold increase in Km for pABA and 3-fold
FT increase in Vmax."
FT /evidence="ECO:0000269|PubMed:31663056"
SQ SEQUENCE 329 AA; 35603 MW; 30BA607BD16A5213 CRC64;
MVIELIINTP SRLHLTLIDL NGERGRLDGG VGITLNEPEL VVGLEASDDM GVEFTSHAEG
KLREEYRSKI MEAARRTLKH IGSDEKFHFT VRSMFPAHSG LGSGTQLSLA TARLVAEYHG
MKFTARELAH IVGRGGTSGI GVASFEDGGF IVDAGHSSRE KSDFLPSSAS SASPPPVIAR
YDFPEEWNII IAIPEIDRSV SGRREVNIFQ EYCPLPLRDV ERLSHIILMK MMPAILEGDI
EAFGESVNEI QGTGFKRIER ELQDPLIDRI IDSMISAGAP GAGMSSFGPA VYSVTDEKPG
NVAGAVAEIM GPGRIIVTGG RNRGAFMIK
