FBIA_MYCTU
ID FBIA_MYCTU Reviewed; 331 AA.
AC P9WP81; L0TET5; P96866; Q7D5T6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Phosphoenolpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_01257, ECO:0000303|PubMed:30952857};
DE EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257, ECO:0000269|PubMed:30952857};
DE AltName: Full=EPPG:FO PEP transferase {ECO:0000255|HAMAP-Rule:MF_01257};
GN Name=fbiA {ECO:0000255|HAMAP-Rule:MF_01257, ECO:0000303|PubMed:30952857};
GN OrderedLocusNames=Rv3261;
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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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 [4]
RP 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).
RN [5]
RP ROLE IN INDUCTION OF MACROPHAGE APOPTOSIS.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=32569876; DOI=10.1016/j.cellimm.2020.104145;
RA Lee K.I., Choi S., Choi H.G., Kebede S.G., Dang T.B., Back Y.W., Park H.S.,
RA Kim H.J.;
RT "Recombinant Rv3261 protein of Mycobacterium tuberculosis induces apoptosis
RT through a mitochondrion-dependent pathway in macrophages and inhibits
RT intracellular bacterial growth.";
RL Cell. Immunol. 354:104145-104145(2020).
CC -!- FUNCTION: Catalyzes the transfer of the phosphoenolpyruvate moiety from
CC enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme
CC F420-0 and GMP. {ECO:0000255|HAMAP-Rule:MF_01257,
CC ECO:0000269|PubMed:30952857}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-didemethyl-8-hydroxy-5-deazariboflavin + enolpyruvoyl-2-
CC diphospho-5'-guanosine = dehydro coenzyme F420-0 + GMP + H(+);
CC Xref=Rhea:RHEA:27510, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:59904, ChEBI:CHEBI:143701, ChEBI:CHEBI:143705;
CC EC=2.7.8.28; Evidence={ECO:0000255|HAMAP-Rule:MF_01257,
CC ECO:0000269|PubMed:30952857};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01257}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC -!- MISCELLANEOUS: Inhibits intracellular mycobacterial growth by inducing
CC apoptosis in infected macrophages. Induces macrophage apoptosis by
CC triggering reactive oxygen species (ROS) production, release of
CC cytochrome c, and activation of caspase-3 via a TLR4-dependent pathway.
CC FbiA-mediated apoptosis may act as a host defense response.
CC {ECO:0000269|PubMed:32569876}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the CofD family. {ECO:0000255|HAMAP-
CC Rule:MF_01257}.
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DR EMBL; AL123456; CCP46080.1; -; Genomic_DNA.
DR PIR; F70977; F70977.
DR RefSeq; NP_217778.1; NC_000962.3.
DR RefSeq; WP_003417087.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WP81; -.
DR SMR; P9WP81; -.
DR STRING; 83332.Rv3261; -.
DR PaxDb; P9WP81; -.
DR DNASU; 888701; -.
DR GeneID; 45427255; -.
DR GeneID; 888701; -.
DR KEGG; mtu:Rv3261; -.
DR TubercuList; Rv3261; -.
DR eggNOG; COG0391; Bacteria.
DR OMA; DLDTVMY; -.
DR PhylomeDB; P9WP81; -.
DR BioCyc; MetaCyc:G185E-7535-MON; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:2001121; P:coenzyme gamma-F420-2 biosynthetic process; IMP:MTBBASE.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07186; CofD_like; 1.
DR Gene3D; 3.40.50.10680; -; 1.
DR HAMAP; MF_01257; CofD; 1.
DR InterPro; IPR002882; CofD.
DR InterPro; IPR038136; CofD-like_dom_sf.
DR InterPro; IPR010115; FbiA/CofD.
DR PANTHER; PTHR43007; PTHR43007; 1.
DR Pfam; PF01933; CofD; 1.
DR SUPFAM; SSF142338; SSF142338; 1.
DR TIGRFAMs; TIGR01819; F420_cofD; 1.
PE 1: Evidence at protein level;
KW Magnesium; Reference proteome; Transferase.
FT CHAIN 1..331
FT /note="Phosphoenolpyruvate transferase"
FT /id="PRO_0000145763"
FT BINDING 63
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
SQ SEQUENCE 331 AA; 35335 MW; 4D144F9A17F792C6 CRC64;
MKVTVLAGGV GGARFLLGVQ QLLGLGQFAA NSAHSDADHQ LSAVVNVGDD AWIHGLRVCP
DLDTCMYTLG GGVDPQRGWG QRDETWHAMQ ELVRYGVQPD WFELGDRDLA THLVRTQMLQ
AGYPLSQITE ALCDRWQPGA RLLPATDDRC ETHVVITDPV DESRKAIHFQ EWWVRYRAQV
PTHSFAFVGA EKSSAATEAI AALADADIIM LAPSNPVVSI GAILAVPGIR AALREATAPI
VGYSPIIGEK PLRGMADTCL SVIGVDSTAA AVGRHYGARC ATGILDCWLV HDGDHAEIDG
VTVRSVPLLM TDPNATAEMV RAGCDLAGVV A
