FBID_CHLSY
ID FBID_CHLSY Reviewed; 205 AA.
AC B9LHE7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=Chy400_0217;
OS Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=480224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29364 / DSM 637 / Y-400-fl;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus sp. Y-400-fl.";
RL Submitted (JAN-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 -!- 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; CP001364; ACM51656.1; -; Genomic_DNA.
DR RefSeq; WP_012256112.1; NC_012032.1.
DR AlphaFoldDB; B9LHE7; -.
DR SMR; B9LHE7; -.
DR KEGG; chl:Chy400_0217; -.
DR HOGENOM; CLU_076569_1_0_0; -.
DR OMA; RCDIDTP; -.
DR OrthoDB; 1930370at2; -.
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..205
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398680"
FT BINDING 138
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 154
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 157
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ SEQUENCE 205 AA; 22501 MW; FA6D51B6999B3DC1 CRC64;
MIGIVIPIKR LHLAKSRLID LLDPADRQQL VVTMVRHVIT TARQAVSYLS IPARIWLVSP
EPTLATDSEG IEWLPDNQEE LNAALTEARQ RIQAAGVQIM MVLAGDLPFV TVRDLILLSE
ALTDNDVVVA PDQHGQGTNA LGLHLPSQLP FGFGPDSAGY HLRTAARLGL RASLISTPTL
AFDLDDGERL QQYYRCIASC DNFAR
