FBID_MYCS2
ID FBID_MYCS2 Reviewed; 221 AA.
AC A0QUZ4; I7FB84;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Phosphoenolpyruvate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE Short=PEP guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE EC=2.7.7.105 {ECO:0000255|HAMAP-Rule:MF_02114};
DE AltName: Full=2-phospho-L-lactate guanylyltransferase;
GN Name=fbiD {ECO:0000255|HAMAP-Rule:MF_02114};
GN OrderedLocusNames=MSMEG_2392, MSMEI_2332;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION IN F420 BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RX PubMed=17660436; DOI=10.1099/mic.0.2006/009241-0;
RA Guerra-Lopez D., Daniels L., Rawat M.;
RT "Mycobacterium smegmatis mc2 155 fbiC and MSMEG_2392 are involved in
RT triphenylmethane dye decolorization and coenzyme F420 biosynthesis.";
RL Microbiology 153:2724-2732(2007).
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:0000255|HAMAP-
CC Rule:MF_02114, ECO:0000269|PubMed:17660436}.
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:0000255|HAMAP-
CC Rule:MF_02114};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02114}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate 7,8-
CC didemethyl-8-hydroxy-5-deazariboflavin (Fo) to five times the wild-type
CC levels but do not produce F420. They are also unable to decolorize
CC triphenylmethane dye, and are sensitive to oxidative stress caused by
CC the redox-cycling agents plumbagin and menadione.
CC {ECO:0000269|PubMed:17660436}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC Rule:MF_02114}.
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DR EMBL; CP000480; ABK73289.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38800.1; -; Genomic_DNA.
DR RefSeq; WP_003893758.1; NZ_SIJM01000012.1.
DR RefSeq; YP_886732.1; NC_008596.1.
DR AlphaFoldDB; A0QUZ4; -.
DR SMR; A0QUZ4; -.
DR STRING; 246196.MSMEI_2332; -.
DR EnsemblBacteria; ABK73289; ABK73289; MSMEG_2392.
DR EnsemblBacteria; AFP38800; AFP38800; MSMEI_2332.
DR GeneID; 66733806; -.
DR KEGG; msg:MSMEI_2332; -.
DR KEGG; msm:MSMEG_2392; -.
DR PATRIC; fig|246196.19.peg.2356; -.
DR eggNOG; COG1920; Bacteria.
DR OMA; RCDIDTP; -.
DR OrthoDB; 1930370at2; -.
DR BRENDA; 1.3.8.17; 3512.
DR BRENDA; 2.7.7.105; 3512.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
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 Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_02114; CofC; 1.
DR InterPro; IPR002835; CofC.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR40392; PTHR40392; 1.
DR Pfam; PF01983; CofC; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR03552; F420_cofC; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..221
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398695"
FT BINDING 154
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 169
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
FT BINDING 172
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02114"
SQ SEQUENCE 221 AA; 22750 MW; 7E231809F648F8B0 CRC64;
MSGRRTPGAA SDGSAGGQAA VIIAVKRLTA AKTRLAPIFS AATREEVVLA MLVDTITAAS
TVAPVTVVTP DEVAADAARQ LGAGVLADPT PEGHHNPLNN AIMAAEEHLR AGTPNIVVLQ
GDLPAMQPRE LAEALAAART YPRSFVGDRH GTGTSALFAF GVPLQPRFGA DSATHHRHSG
AIELTGAWPG LRCDIDTAED LRTARRLGVG PATAQAIAAH R
