FBID_MYCGI
ID FBID_MYCGI Reviewed; 214 AA.
AC A4TE28;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, 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=Mflv_4222;
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL Submitted (APR-2007) 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; CP000656; ABP46691.1; -; Genomic_DNA.
DR RefSeq; WP_011895066.1; NC_009338.1.
DR AlphaFoldDB; A4TE28; -.
DR SMR; A4TE28; -.
DR STRING; 350054.Mflv_4222; -.
DR EnsemblBacteria; ABP46691; ABP46691; Mflv_4222.
DR KEGG; mgi:Mflv_4222; -.
DR eggNOG; COG1920; Bacteria.
DR HOGENOM; CLU_076569_0_0_11; -.
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..214
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398690"
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; 21973 MW; E63FEC758DFC329A CRC64;
MRNSAPDADI GLVIAVKRLT AAKTRLAPVL SATNRESVVL AMLVDTIGAA ITVPAVRSVL
VVTPDDGAAS AARRLGARVL ADPTPAGHRD PLNNALSAAE TAIREECSNI VVLQGDLPAL
KSIELAEALH AARAHPRSFV TDRHGTGTAA LFAFGVALQP RFGAGSAQRH RESGAVELTG
DWPGLRSDID TPEDLVAACE LGVGPATSQA ISAA
