ID M2PRS5_9PSEU Unreviewed; 208 AA.
AC M2PRS5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=C791_0315 {ECO:0000313|EMBL:EMD22235.1};
OS Amycolatopsis azurea DSM 43854.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1238180 {ECO:0000313|EMBL:EMD22235.1, ECO:0000313|Proteomes:UP000014137};
RN [1] {ECO:0000313|EMBL:EMD22235.1, ECO:0000313|Proteomes:UP000014137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43854 {ECO:0000313|EMBL:EMD22235.1,
RC ECO:0000313|Proteomes:UP000014137};
RA Khatri I., Kaur I., Subramanian S., Mayilraj S.;
RT "Genome assembly of Amycolatopsis azurea DSM 43854.";
RL Submitted (OCT-2012) 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:EMD22235.1}.
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DR EMBL; ANMG01000101; EMD22235.1; -; Genomic_DNA.
DR AlphaFoldDB; M2PRS5; -.
DR PATRIC; fig|1238180.3.peg.8046; -.
DR OrthoDB; 9151145at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000014137; 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:EMD22235.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:EMD22235.1}.
FT BINDING 138
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 153
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 156
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
SQ SEQUENCE 208 AA; 21500 MW; AAC35B64B095394A CRC64;
MGIDLIVPMK RPAEGKSRLR GAVVPERHAE LVLALAYDTL SAATSADGIR RVLVVAADPA
SVADLTELGV EIVPEPSRGG LNAALRYGEE LLRRDTPSVL VGALQADLPA LRTEDLTAAL
VEAAGRRAFV ADRQGTGTTL LLAGAGPLEP RFGEGSARAH TASGATPLTI APESLRADVD
TADDLAHVRT LGVGKRSSTL LGTPCVVM
//
