RFHPS_METJA
ID RFHPS_METJA Reviewed; 328 AA.
AC Q58822;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Beta-ribofuranosylphenol 5'-phosphate synthase {ECO:0000305};
DE EC=2.4.2.54 {ECO:0000269|PubMed:21634403};
DE AltName: Full=Beta-ribofuranosylaminobenzene 5'-phosphate synthase {ECO:0000305};
DE Short=Beta-RFA-P synthase {ECO:0000303|PubMed:15262968};
DE AltName: Full=Beta-ribofuranosylhydroxybenzene 5'-phosphate synthase {ECO:0000305};
DE Short=Beta-RFH-P synthase {ECO:0000303|PubMed:21634403};
GN OrderedLocusNames=MJ1427;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ENZYME MECHANISM, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=15262968; DOI=10.1074/jbc.m406442200;
RA Dumitru R.V., Ragsdale S.W.;
RT "Mechanism of 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate synthase, a
RT key enzyme in the methanopterin biosynthetic pathway.";
RL J. Biol. Chem. 279:39389-39395(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21634403; DOI=10.1021/bi200362w;
RA White R.H.;
RT "The conversion of a phenol to an aniline occurs in the biochemical
RT formation of the 1-(4-aminophenyl)-1-deoxy-D-ribitol moiety in
RT methanopterin.";
RL Biochemistry 50:6041-6052(2011).
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) (PubMed:21634403). Also
CC catalyzes the condensation of 4-aminobenzoate (pABA) with PRPP to
CC produce beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P)
CC (PubMed:15262968, PubMed:21634403). Only 4-hydroxybenzoate is known to
CC be biosynthesized by methanogenic archaea, but 4-aminobenzoate can be
CC used as substrate by growing methanogens when it is present in the
CC growth medium (PubMed:21634403). {ECO:0000269|PubMed:15262968,
CC ECO:0000269|PubMed:21634403}.
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:0000269|PubMed:21634403};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48557;
CC Evidence={ECO:0000269|PubMed:21634403};
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:15262968, ECO:0000269|PubMed:21634403};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35816;
CC Evidence={ECO:0000269|PubMed:15262968, ECO:0000269|PubMed:21634403};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15262968};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for PRPP {ECO:0000269|PubMed:15262968};
CC KM=0.15 mM for pABA {ECO:0000269|PubMed:15262968};
CC Vmax=180 nmol/min/mg enzyme with pABA as substrate
CC {ECO:0000269|PubMed:15262968};
CC Note=kcat is 0.23 sec(-1) with pABA as substrate.
CC {ECO:0000269|PubMed:15262968};
CC pH dependence:
CC Optimum pH is 4.9. {ECO:0000269|PubMed:15262968};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000305|PubMed:15262968,
CC ECO:0000305|PubMed:21634403}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15262968}.
CC -!- MISCELLANEOUS: Lacks any chromogenic cofactor, and the presence of
CC pyridoxal phosphate and the mechanistically related pyruvoyl cofactors
CC has been strictly excluded. {ECO:0000269|PubMed:15262968}.
CC -!- SIMILARITY: Belongs to the beta-RFA-P synthase family. {ECO:0000305}.
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DR EMBL; L77117; AAB99449.1; -; Genomic_DNA.
DR PIR; B64478; B64478.
DR RefSeq; WP_010870945.1; NC_000909.1.
DR AlphaFoldDB; Q58822; -.
DR SMR; Q58822; -.
DR STRING; 243232.MJ_1427; -.
DR EnsemblBacteria; AAB99449; AAB99449; MJ_1427.
DR GeneID; 1452331; -.
DR KEGG; mja:MJ_1427; -.
DR eggNOG; arCOG01026; Archaea.
DR HOGENOM; CLU_061764_0_0_2; -.
DR InParanoid; Q58822; -.
DR OMA; RLNGAWY; -.
DR OrthoDB; 47243at2157; -.
DR PhylomeDB; Q58822; -.
DR BioCyc; MetaCyc:MON-14546; -.
DR BRENDA; 2.4.2.54; 3260.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000000805; 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; 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; 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..328
FT /note="Beta-ribofuranosylphenol 5'-phosphate synthase"
FT /id="PRO_0000107320"
SQ SEQUENCE 328 AA; 36198 MW; 67F166A355C41FA1 CRC64;
MIIQTPSRIH MGLIDLNGSI GRVDGGIGLA LEEPNIKIEG KESDDISIEF DKKLIEKYGE
DYIKSVRDRV YNTAIKVLDV IGGEGVDLKI LSLFPAHSGL GSGTQLSLAV GKLISKIYNK
EMNAYNIAKI TGRGGTSGIG IGAFEYGGFL IDGGHSFGKG KDKEDFRPSS ASKGVKPAPI
IFRHDFDWET ILIIPKGEHV YGKKEVDIFK KYCPVPLNEV EKICHLVLMK MMPAVVEKNL
DDFGEVINKL QYLGFKKVEL SLQSDIVKDL INELHKDVYA GLSSFGPTIY AFGDKKLIVE
KANDIFDKYG VYGEIIITKA NNVGHKIW
