ID A0A1I6HUH7_9EURY Unreviewed; 325 AA.
AC A0A1I6HUH7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Beta-ribofuranosylaminobenzene 5'-phosphate synthase {ECO:0000256|PIRNR:PIRNR004884};
DE Short=Beta-RFA-P synthase {ECO:0000256|PIRNR:PIRNR004884};
DE EC=2.4.2.54 {ECO:0000256|PIRNR:PIRNR004884};
GN ORFNames=SAMN04487947_2522 {ECO:0000313|EMBL:SFR58105.1};
OS Halogeometricum rufum.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=553469 {ECO:0000313|EMBL:SFR58105.1, ECO:0000313|Proteomes:UP000198531};
RN [1] {ECO:0000313|EMBL:SFR58105.1, ECO:0000313|Proteomes:UP000198531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7736 {ECO:0000313|EMBL:SFR58105.1,
RC ECO:0000313|Proteomes:UP000198531};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of 4-aminobenzoate (pABA) with 5-
CC phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce beta-
CC ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P).
CC {ECO:0000256|PIRNR:PIRNR004884}.
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:0000256|PIRNR:PIRNR004884};
CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin
CC biosynthesis. {ECO:0000256|PIRNR:PIRNR004884}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR004884}.
CC -!- SIMILARITY: Belongs to the beta-RFA-P synthase family.
CC {ECO:0000256|PIRNR:PIRNR004884}.
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DR EMBL; FOYT01000002; SFR58105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6HUH7; -.
DR STRING; 553469.SAMN04487947_2522; -.
DR OrthoDB; 85156at2157; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000198531; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-UniRule.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00144; beta_RFAP_syn; 1.
DR PANTHER; PTHR20861:SF6; BETA-RIBOFURANOSYLPHENOL 5'-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR20861; HOMOSERINE/4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE; 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; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR004884};
KW Transferase {ECO:0000256|PIRNR:PIRNR004884}.
FT DOMAIN 74..134
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 217..300
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
SQ SEQUENCE 325 AA; 33776 MW; EE3454816B37C1DD CRC64;
MSRVRVSTGA RLHFGFLNLS LAHQRLYGGL GVGLDEPRTV VAAEPATEID CPDADARAYV
ERAVDALDVP GAAVAVESAL PRHAGLGSGT QLALAVLEAV ARAHDRTVSV RELAPRLGRG
GRSGIGVAAF EDGGVLVDGG HPTARFTTDR PADGDWTVPP VAVRHAVPDD WRFVVVVPDA
DSGRSGEEED ESMRSVVERA DPGVADRISG VLSRRLLPAV ADGSAARFGE AVSEIGRLNG
AWYADEQGGV YRPPVGELVA SLEDDPACYG AGQSSWGPAV YAVTDADHAD AARAAGRAAL
DAADVAGEVR LVRGRNEGAT IRRNG
//
