FBID_NOCFA
ID FBID_NOCFA Reviewed; 226 AA.
AC Q5YRY5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=NFA_42070;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD59056.1; -; Genomic_DNA.
DR RefSeq; WP_011210741.1; NC_006361.1.
DR AlphaFoldDB; Q5YRY5; -.
DR SMR; Q5YRY5; -.
DR STRING; 247156.NFA_42070; -.
DR EnsemblBacteria; BAD59056; BAD59056; NFA_42070.
DR GeneID; 61134841; -.
DR KEGG; nfa:NFA_42070; -.
DR eggNOG; COG1920; Bacteria.
DR HOGENOM; CLU_076569_0_0_11; -.
DR OMA; RCDIDTP; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000006820; 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..226
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398702"
FT BINDING 145
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 161
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 164
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ SEQUENCE 226 AA; 23324 MW; F9A88EAFD4CB079A CRC64;
MRPHAVHALI AVKRLDQAKS RLADRLRPEH RARLVLAMLA DTMTATTSVP GIAAVTVVTP
DAAVADLARS LGGHVHPEPA ADSADSLNAA LAAAAAGVRA RHGGVDLLAL QADLPALRPD
ELADVLATAP RGGRAIVTDH AGTGTAALLV RDGGELAPAF GPDSARRHIA AGAVDLPGEW
PGLRRDVDTA ADLERAVELG AGSSTRALLR DIGWSCRVHE PARRVC
