ID   FBID_THET1              Reviewed;         230 AA.
AC   D1CDA4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Tter_1863;
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Chloroflexi; Thermobaculum.
OX   NCBI_TaxID=525904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1;
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA   Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA   Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ42769.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1CDA4; -.
DR   SMR; D1CDA4; -.
DR   STRING; 525904.Tter_1863; -.
DR   EnsemblBacteria; ACZ42769; ACZ42769; Tter_1863.
DR   KEGG; ttr:Tter_1863; -.
DR   eggNOG; COG1920; Bacteria.
DR   HOGENOM; CLU_076569_1_0_0; -.
DR   OMA; RCDIDTP; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000323; Chromosome 1.
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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..230
FT                   /note="Phosphoenolpyruvate guanylyltransferase"
FT                   /id="PRO_0000398719"
FT   BINDING         139
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT   BINDING         155
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT   BINDING         158
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ   SEQUENCE   230 AA;  25358 MW;  447DEF2FBBA9F924 CRC64;
     MSAMNIAVLV PVKKLDKAKM RMADTLDRSQ RRQLMMVTLR RVLSALQKAQ IGDVYLVASD
     PQVKNIACDL CVKFIPDQGD ELNPSLELAR GELCQNYDAL LVVFGDLPMI SDKDIKTIVR
     LGSSKPSCVI APDKRNVGTN VLFLHPPYLL PFTFGGNSYE RFRSNCEKLG VQFLVYQSQN
     TALDLDYPQD ILDLAALRGH KISGLEEILD PGVLAQISQV TSMSGAKMGA