ID   FBID_CONWI              Reviewed;         223 AA.
AC   D3F5L6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=Cwoe_4150;
OS   Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS   100937 / ID131577).
OC   Bacteria; Actinobacteria; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; CP001854; ADB52565.1; -; Genomic_DNA.
DR   RefSeq; WP_012935616.1; NC_013739.1.
DR   AlphaFoldDB; D3F5L6; -.
DR   SMR; D3F5L6; -.
DR   STRING; 469383.Cwoe_4150; -.
DR   EnsemblBacteria; ADB52565; ADB52565; Cwoe_4150.
DR   KEGG; cwo:Cwoe_4150; -.
DR   eggNOG; COG1920; Bacteria.
DR   HOGENOM; CLU_076569_1_0_11; -.
DR   OMA; RCDIDTP; -.
DR   OrthoDB; 1930370at2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000008229; Chromosome.
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..223
FT                   /note="Phosphoenolpyruvate guanylyltransferase"
FT                   /id="PRO_0000398683"
FT   BINDING         140
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"
FT   BINDING         159
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ   SEQUENCE   223 AA;  23602 MW;  2AFF1D2EF36CDBA9 CRC64;
     MSTFAILPVK RFEGAKGRLA GGLAAGPRRA LAEAMYVDVL TALRRTQGVD RVLVLTADPG
     AQRVAEGYDA IPLDDPAEAG QNRAVMRGVA HARELGATRV LCLSGDTPML DPADLDALLG
     RPRTADRYVV IVPDRHGEGT NGLLLCPPDG MKPSYGVDSC ARHKALAEEA GLAVEIAEIP
     SVALDVDTPD DLDALRELIA SRRGGAAHTR GMLNQLLRTN PKN