FBID_MYCTU
ID FBID_MYCTU Reviewed; 214 AA.
AC P9WP83; L0TDZ2; P95112; Q7D6B3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Phosphoenolpyruvate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114, ECO:0000303|PubMed:30952857};
DE Short=PEP guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE EC=2.7.7.105 {ECO:0000255|HAMAP-Rule:MF_02114, ECO:0000269|PubMed:30952857};
GN Name=fbiD {ECO:0000255|HAMAP-Rule:MF_02114, ECO:0000303|PubMed:30952857};
GN OrderedLocusNames=Rv2983;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 2-214 IN APOFORM AND IN COMPLEX
RP WITH PEP, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30952857; DOI=10.1038/s41467-019-09534-x;
RA Bashiri G., Antoney J., Jirgis E.N.M., Shah M.V., Ney B., Copp J.,
RA Stuteley S.M., Sreebhavan S., Palmer B., Middleditch M., Tokuriki N.,
RA Greening C., Scott C., Baker E.N., Jackson C.J.;
RT "A revised biosynthetic pathway for the cofactor F420 in prokaryotes.";
RL Nat. Commun. 10:1558-1558(2019).
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:30952857}.
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, ECO:0000269|PubMed:30952857};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02114}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC Rule:MF_02114}.
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DR EMBL; AL123456; CCP45788.1; -; Genomic_DNA.
DR PIR; D70673; D70673.
DR RefSeq; NP_217499.1; NC_000962.3.
DR RefSeq; WP_003415094.1; NZ_NVQJ01000099.1.
DR PDB; 6BWG; X-ray; 1.99 A; A/B/C=2-214.
DR PDB; 6BWH; X-ray; 2.18 A; A/B/C=2-214.
DR PDBsum; 6BWG; -.
DR PDBsum; 6BWH; -.
DR AlphaFoldDB; P9WP83; -.
DR SMR; P9WP83; -.
DR STRING; 83332.Rv2983; -.
DR PaxDb; P9WP83; -.
DR DNASU; 888161; -.
DR GeneID; 45426972; -.
DR GeneID; 888161; -.
DR KEGG; mtu:Rv2983; -.
DR TubercuList; Rv2983; -.
DR eggNOG; COG1920; Bacteria.
DR OMA; RCDIDTP; -.
DR BioCyc; MetaCyc:G185E-7238-MON; -.
DR BRENDA; 2.7.7.105; 3445.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001584; 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 3D-structure; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..214
FT /note="Phosphoenolpyruvate guanylyltransferase"
FT /id="PRO_0000398696"
FT BINDING 148
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:30952857"
FT BINDING 163
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:30952857"
FT BINDING 166
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:30952857"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:6BWG"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 32..50
FT /evidence="ECO:0007829|PDB:6BWG"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:6BWG"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6BWG"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:6BWG"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6BWG"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:6BWG"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:6BWG"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:6BWG"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:6BWG"
SQ SEQUENCE 214 AA; 21819 MW; 207508F4E007629E CRC64;
MSGTPDDGDI GLIIAVKRLA AAKTRLAPVF SAQTRENVVL AMLVDTLTAA AGVGSLRSIT
VITPDEAAAA AAAGLGADVL ADPTPEDDPD PLNTAITAAE RVVAEGASNI VVLQGDLPAL
QTQELAEAIS AARHHRRSFV ADRLGTGTAV LCAFGTALHP RFGPDSSARH RRSGAVELTG
AWPGLRCDVD TPADLTAARQ LGVGPATARA VAHR
