ID A0A132MP59_9ACTN Unreviewed; 224 AA.
AC A0A132MP59;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=LI90_1271 {ECO:0000313|EMBL:KWW99632.1}, TH66_08525
GN {ECO:0000313|EMBL:KWX03993.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99632.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|EMBL:KWX03993.1, ECO:0000313|Proteomes:UP000070659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UBT1 {ECO:0000313|EMBL:KWX03993.1,
RC ECO:0000313|Proteomes:UP000070659};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KWW99632.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:KWW99632.1};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Woodward J., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-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:KWW99632.1}.
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DR EMBL; LAXD01000001; KWW99632.1; -; Genomic_DNA.
DR EMBL; JYIJ01000016; KWX03993.1; -; Genomic_DNA.
DR RefSeq; WP_066885330.1; NZ_LAXD01000001.1.
DR AlphaFoldDB; A0A132MP59; -.
DR STRING; 1469144.LI90_1271; -.
DR PATRIC; fig|1469144.10.peg.1402; -.
DR OrthoDB; 9151145at2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000070188; Unassembled WGS sequence.
DR Proteomes; UP000070659; 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:KWW99632.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:KWW99632.1}.
FT BINDING 147
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 163
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
FT BINDING 166
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02114"
SQ SEQUENCE 224 AA; 22843 MW; 83855B91EDCD82FD CRC64;
MVFPTSTAPP SWCLVVPVKL LAHAKTRLAG LAGARRAELA LAFAADTITA ALRCPRVVEV
IAVSDDPRAR ELLTGLGATV VPDEPDAGLN PALAHGAAVA SERRPACGVA ALSADLPALR
PDELARALDA AAGHRRAFVP DAAGVGTTLL AAAPRAPLEP AFGGRSRDRH RHQGAYELVL
PGIDSVRRDV DTEADLAAAL ALGVGARTAA VLAELGGSPR PAEP
//
