ID A0A0E3L5U8_9EURY Unreviewed; 307 AA.
AC A0A0E3L5U8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=MSMTP_0427 {ECO:0000313|EMBL:AKB23896.1};
OS Methanosarcina sp. MTP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434100 {ECO:0000313|EMBL:AKB23896.1, ECO:0000313|Proteomes:UP000033049};
RN [1] {ECO:0000313|EMBL:AKB23896.1, ECO:0000313|Proteomes:UP000033049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTP4 {ECO:0000313|EMBL:AKB23896.1,
RC ECO:0000313|Proteomes:UP000033049};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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; CP009505; AKB23896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3L5U8; -.
DR STRING; 1434100.MSMTP_0427; -.
DR KEGG; metm:MSMTP_0427; -.
DR PATRIC; fig|1434100.4.peg.556; -.
DR HOGENOM; CLU_061764_0_0_2; -.
DR UniPathway; UPA00065; -.
DR Proteomes; UP000033049; Chromosome.
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; 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 NCBIfam; NF040726; BetaRFA-P_synth; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000033049};
KW Transferase {ECO:0000256|PIRNR:PIRNR004884}.
FT DOMAIN 63..124
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
SQ SEQUENCE 307 AA; 32963 MW; A7AC88B0EFDB2375 CRC64;
MTLIDLNGEI GRVDGGAGLA LPTPNVTLTA EKADEIRVEG AEAFTDRMKR AVEAVLPEGE
GVRINVESLI PPHVGFGSGT QSSLSAAAAV NELYGLGMSV RDLAFTVQRG GTSGIGVGAF
ENGGFIVDGG HRFRDKGAFL PSAASRVPPG PVLFRRDFPD WNLVVAVPND KGMHDEEEVA
VFKKFCPLPI EEVREVAHVV LMQMMPAVME EDIESFGSAV NHVQNVGFNR LEHYVWPDIV
KEVSAFMRTR SYGAGVSSFG PVVYSLVDNK AEGQELQAEV QQMLDESLGG TVFMTKAKNS
GAEISRL
//
