ID A0A1I2K5E5_9ACTN Unreviewed; 248 AA.
AC A0A1I2K5E5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216251_121124 {ECO:0000313|EMBL:SFF62124.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF62124.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFF62124.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF62124.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FONG01000021; SFF62124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2K5E5; -.
DR STRING; 380248.SAMN05216251_121124; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000199323; 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; IPR025877; MobA-like_NTP_Trfase.
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; PF12804; NTP_transf_3; 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:SFF62124.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:SFF62124.1}.
FT DOMAIN 73..181
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 192
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 195
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
SQ SEQUENCE 248 AA; 24945 MW; 79A958BEA4E7E9C4 CRC64;
MRQPHKSAAK HTLMPGPGRP RGAGDRPHNG AVAIDVTWKW SLVVPLKPLE VAKSRLARAA
GAVRPALALA FALDTVAAAL ACAEVGDVTV VTDDGRAGAE LAALGAFVVP DAPAGGLNAA
LRYGAARVRG RDPYAAVAAL NGDLPALRPA ELSQVLREAA GAQGRAFLAD AAGVGTTLLA
APRGSALSPA FGGPSRARHL ATGAREITLP HVASVRQDVD TGDDLRAALA LGVGERTALA
ASGLLIAD
//
