ID   FBIA_MYCBO              Reviewed;         331 AA.
AC   Q7TWV4; A0A1R3Y3X0; X2BNV9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Phosphoenolpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_01257};
DE            EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257};
DE   AltName: Full=EPPG:FO PEP transferase {ECO:0000255|HAMAP-Rule:MF_01257};
GN   Name=fbiA {ECO:0000255|HAMAP-Rule:MF_01257}; Synonyms=cofD;
GN   OrderedLocusNames=BQ2027_MB3289;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   ROLE IN COENZYME F420 BIOSYNTHESIS.
RC   STRAIN=BCG;
RX   PubMed=11717263; DOI=10.1128/jb.183.24.7058-7066.2001;
RA   Choi K.-P., Bair T.B., Bae Y.-M., Daniels L.;
RT   "Use of transposon Tn5367 mutagenesis and a nitroimidazopyran-based
RT   selection system to demonstrate a requirement for fbiA and fbiB in coenzyme
RT   F(420) biosynthesis by Mycobacterium bovis BCG.";
RL   J. Bacteriol. 183:7058-7066(2001).
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   -!- 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   -!- 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, ECO:0000305|PubMed:11717263}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- SIMILARITY: Belongs to the CofD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01257, ECO:0000305}.
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DR   EMBL; LT708304; SIU01918.1; -; Genomic_DNA.
DR   RefSeq; NP_856934.1; NC_002945.3.
DR   RefSeq; WP_003417087.1; NC_002945.4.
DR   AlphaFoldDB; Q7TWV4; -.
DR   SMR; Q7TWV4; -.
DR   EnsemblBacteria; SIU01918; SIU01918; BQ2027_MB3289.
DR   GeneID; 45427255; -.
DR   PATRIC; fig|233413.5.peg.3616; -.
DR   OMA; DLDTVMY; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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   3: Inferred from homology;
KW   Magnesium; Transferase.
FT   CHAIN           1..331
FT                   /note="Phosphoenolpyruvate transferase"
FT                   /id="PRO_0000145760"
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