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Entry: A0A0T1WKJ3_9MYCO
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Original site: A0A0T1WKJ3_9MYCO 
ID   A0A0T1WKJ3_9MYCO        Unreviewed;       216 AA.
AC   A0A0T1WKJ3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=ASD37_05925 {ECO:0000313|EMBL:KQY09903.1};
OS   Mycobacterium sp. Root135.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY09903.1, ECO:0000313|Proteomes:UP000051127};
RN   [1] {ECO:0000313|EMBL:KQY09903.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY09903.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY09903.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY09903.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQY09903.1}.
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DR   EMBL; LMEZ01000001; KQY09903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0T1WKJ3; -.
DR   STRING; 1736457.ASD37_05925; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000051127; 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:KQY09903.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051127};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:KQY09903.1}.
FT   BINDING         150
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT   BINDING         165
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT   BINDING         168
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
SQ   SEQUENCE   216 AA;  22349 MW;  01BCE1F5558E0653 CRC64;
     MSGPSSVRTA NLGLIIAVKR LSDAKTRLAS AFSPGDREGV VLAMLLDTIT AASSVMAVRT
     ITVVTPDPVA AEAVRELGAH VFVDPTPAGH PDPLNNAISV TEAAIRAETP NVGVLQGDLP
     ALQPRELAEA IAQARHHQRS FVSDRHGTGT SALFAFGVPL ASVLGTDSAR RHKDSRAVEL
     TGRWPGLRCD IDTPDDLATA LGLGVGALTK NTVGGT
//
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