ID   FBIA_MYCTA              Reviewed;         331 AA.
AC   A5U7T5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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}; OrderedLocusNames=MRA_3302;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- SIMILARITY: Belongs to the CofD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01257}.
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DR   EMBL; CP000611; ABQ75085.1; -; Genomic_DNA.
DR   RefSeq; WP_003417087.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U7T5; -.
DR   SMR; A5U7T5; -.
DR   STRING; 419947.MRA_3302; -.
DR   EnsemblBacteria; ABQ75085; ABQ75085; MRA_3302.
DR   GeneID; 45427255; -.
DR   KEGG; mra:MRA_3302; -.
DR   eggNOG; COG0391; Bacteria.
DR   HOGENOM; CLU_055795_0_0_11; -.
DR   OMA; DLDTVMY; -.
DR   OrthoDB; 1079756at2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001988; 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_1000067255"
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