ID   FBID_MYCSS              Reviewed;         218 AA.
AC   Q1BAP9;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Mmcs_1926;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) 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; CP000384; ABG08035.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BAP9; -.
DR   SMR; Q1BAP9; -.
DR   KEGG; mmc:Mmcs_1926; -.
DR   HOGENOM; CLU_076569_0_0_11; -.
DR   OMA; RCDIDTP; -.
DR   BioCyc; MSP164756:G1G6O-1970-MON; -.
DR   UniPathway; UPA00071; -.
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; Transferase.
FT   CHAIN           1..218
FT                   /note="Phosphoenolpyruvate guanylyltransferase"
FT                   /id="PRO_5000124151"
FT   BINDING         151
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT   BINDING         166
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT   BINDING         169
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ   SEQUENCE   218 AA;  22267 MW;  3286A18FFD27F9CD CRC64;
     MRGTTSNGAA PSGAGVAVVI AVKRLADAKT RLAPIFAPHD RETVVLAMLV DTVAAAAAVA
     AVTVVTPDPA AAEAARALGA QVLDDPTPAG HPDPLNNALR AAEAAVRATV PNVVALQGDL
     PALQAQELSE AIAAARTRPR SFVGDRHGTG TSALFAFGVP LDPRFGPDSA ERHRRSGAVE
     LTGSWPGLRY DIDTPDDLLA ARRLGVGTQT ARAVGAER