FBID_THERP
ID FBID_THERP Reviewed; 200 AA.
AC B9L4T8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Phosphoenolpyruvate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE Short=PEP guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE EC=2.7.7.105 {ECO:0000255|HAMAP-Rule:MF_02114};
GN Name=fbiD {ECO:0000255|HAMAP-Rule:MF_02114}; OrderedLocusNames=trd_A0802;
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OG Plasmid Tros.
OC Bacteria; Chloroflexi; Thermomicrobiales; Thermomicrobiaceae;
OC Thermomicrobium.
OX NCBI_TaxID=309801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2;
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
CC -!- FUNCTION: Guanylyltransferase that catalyzes the activation of
CC phosphoenolpyruvate (PEP) as enolpyruvoyl-2-diphospho-5'-guanosine, via
CC the condensation of PEP with GTP. It is involved in the biosynthesis of
CC coenzyme F420, a hydride carrier cofactor. {ECO:0000255|HAMAP-
CC Rule:MF_02114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H(+) + phosphoenolpyruvate = diphosphate + enolpyruvoyl-
CC 2-diphospho-5'-guanosine; Xref=Rhea:RHEA:30519, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:143701; EC=2.7.7.105; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02114};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02114}.
CC -!- MISCELLANEOUS: The exact nature of the substrate is currently not
CC known. This entry has been annotated based on its similarity to
CC Actinobacteria. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC Rule:MF_02114}.
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DR EMBL; CP001276; ACM06659.1; -; Genomic_DNA.
DR RefSeq; WP_012642646.1; NC_011961.1.
DR AlphaFoldDB; B9L4T8; -.
DR SMR; B9L4T8; -.
DR STRING; 309801.trd_A0802; -.
DR EnsemblBacteria; ACM06659; ACM06659; trd_A0802.
DR KEGG; tro:trd_A0802; -.
DR eggNOG; COG1920; Bacteria.
DR HOGENOM; CLU_076569_1_0_0; -.
DR OMA; RCDIDTP; -.
DR OrthoDB; 1930370at2; -.
DR BRENDA; 2.7.7.105; 6311.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000447; Plasmid Tros.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:InterPro.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_02114; CofC; 1.
DR InterPro; IPR002835; CofC.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR40392; PTHR40392; 1.
DR Pfam; PF01983; CofC; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR03552; F420_cofC; 1.
PE 3: Inferred from homology;
KW GTP-binding; Nucleotide-binding; Nucleotidyltransferase; Plasmid;
KW Transferase.
FT CHAIN 1..200
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398720"
FT BINDING 137
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 153
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 156
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ SEQUENCE 200 AA; 21668 MW; 87ACD2DADA5E3637 CRC64;
MQVLAVVPVQ RLEQAKSRLA PALEPAARQA LVRELAERTI RILRSVPAVA VIGLLTPDPS
LASLASRWGV RTLRDAAHGL NDAVRLAQAE ACRLHLPALL IVLGDLPLLD PHAIRHALAL
LESPGVVLAP DRHGTGTNLL ALAPPDVIAP AFGPFSRWRH RRAAAGARCT IRELWSRALV
LDLDTPEDLA LVHRVREGER
