FBID_RHOOB
ID FBID_RHOOB Reviewed; 240 AA.
AC C1B2N5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=ROP_65550;
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=632772;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4;
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-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}.
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DR EMBL; AP011115; BAH54802.1; -; Genomic_DNA.
DR RefSeq; WP_015890248.1; NC_012522.1.
DR AlphaFoldDB; C1B2N5; -.
DR SMR; C1B2N5; -.
DR STRING; 632772.ROP_65550; -.
DR EnsemblBacteria; BAH54802; BAH54802; ROP_65550.
DR KEGG; rop:ROP_65550; -.
DR PATRIC; fig|632772.20.peg.6841; -.
DR HOGENOM; CLU_076569_0_0_11; -.
DR OMA; RCDIDTP; -.
DR OrthoDB; 1930370at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000002212; 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; Transferase.
FT CHAIN 1..240
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398706"
FT BINDING 161
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 178
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 181
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ SEQUENCE 240 AA; 24435 MW; A8B5EA258CCD04C6 CRC64;
MSTATRSVAP RAHVLVAVKE LHAAKTRLSG VFDTDDRTGL VLSMLRDTLA VVSDVATVVG
VTVVTPDPAV ARLARSVGAH VYADPAPVAA GDPADEGGTE HGLNAALAAA AEHVRRNESG
VDVVALQADL PSLRGGEFGE ALAAARTGGR SVVVDHHGTG TAALFSCDPE VPLDPRFGPG
SAKRHLESGA RPLDGHWPGL RTDVDTADDL DAAQALGVGP ATRAALDALE HSAPSHCGNE
