ID   FBID_MYCTK              Reviewed;         214 AA.
AC   C6DW66;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
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=TBMG_00986;
OS   Mycobacterium tuberculosis (strain KZN 1435 / MDR).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=478434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KZN 1435 / MDR;
RA   Murray M., Pillay M., Borowsky M.L., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I., Hepburn T.A.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Nusbaum C., Galagan J., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis strain KZN 1435.";
RL   Submitted (JUL-2009) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACT24030.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001658; ACT24030.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003415094.1; NZ_KK341220.1.
DR   AlphaFoldDB; C6DW66; -.
DR   SMR; C6DW66; -.
DR   GeneID; 45426972; -.
DR   KEGG; mtb:TBMG_00986; -.
DR   PATRIC; fig|478434.13.peg.3222; -.
DR   HOGENOM; CLU_076569_0_0_11; -.
DR   OMA; RCDIDTP; -.
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..214
FT                   /note="Phosphoenolpyruvate guanylyltransferase"
FT                   /id="PRO_0000398699"
FT   BINDING         148
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT   BINDING         163
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"
SQ   SEQUENCE   214 AA;  21819 MW;  207508F4E007629E CRC64;
     MSGTPDDGDI GLIIAVKRLA AAKTRLAPVF SAQTRENVVL AMLVDTLTAA AGVGSLRSIT
     VITPDEAAAA AAAGLGADVL ADPTPEDDPD PLNTAITAAE RVVAEGASNI VVLQGDLPAL
     QTQELAEAIS AARHHRRSFV ADRLGTGTAV LCAFGTALHP RFGPDSSARH RRSGAVELTG
     AWPGLRCDVD TPADLTAARQ LGVGPATARA VAHR