ID D5PIZ0_9MYCO Unreviewed; 220 AA.
AC D5PIZ0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Phosphoenolpyruvate guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE Short=PEP guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE EC=2.7.7.105 {ECO:0000256|HAMAP-Rule:MF_02114};
GN Name=fbiD {ECO:0000256|HAMAP-Rule:MF_02114};
GN ORFNames=HMPREF0591_6134 {ECO:0000313|EMBL:EFG74014.1};
OS Mycobacterium parascrofulaceum ATCC BAA-614.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=525368 {ECO:0000313|EMBL:EFG74014.1, ECO:0000313|Proteomes:UP000003653};
RN [1] {ECO:0000313|EMBL:EFG74014.1, ECO:0000313|Proteomes:UP000003653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-614 {ECO:0000313|EMBL:EFG74014.1,
RC ECO:0000313|Proteomes:UP000003653};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (APR-2010) 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:0000256|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:0000256|HAMAP-
CC Rule:MF_02114};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02114}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000256|HAMAP-
CC Rule:MF_02114}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFG74014.1}.
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DR EMBL; ADNV01000389; EFG74014.1; -; Genomic_DNA.
DR AlphaFoldDB; D5PIZ0; -.
DR eggNOG; COG1920; Bacteria.
DR HOGENOM; CLU_076569_0_0_11; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000003653; Unassembled WGS sequence.
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 HAMAP; MF_02114; CofC; 1.
DR InterPro; IPR002835; CofC.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR03552; F420_cofC; 1.
DR PANTHER; PTHR40392; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR PANTHER; PTHR40392:SF1; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR Pfam; PF01983; CofC; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_02114,
KW ECO:0000313|EMBL:EFG74014.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:EFG74014.1}.
FT BINDING 154
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 169
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 172
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
SQ SEQUENCE 220 AA; 22515 MW; 8B9B1602921D0AD2 CRC64;
MASMSGTRAD EGGRDVALIV AVKRLAAAKT RLAPVFSART RESVVLAMLM DTLTAAGRVA
ALGSITVITP DEAAAAAATE LGAEVLADPT PEGHADPLNN AIATAERAVG GFFPNVVVLQ
GDLPALQTQE LAEAIAAARH HRRSFVADRL ATGTAALFAF GAALDPQFGS DSSARHRRSG
AIELTGAWPG LRCDVDTPDD LAAARRLGVG AATARALAQQ
//
