ID   FBIA_MYCMM              Reviewed;         329 AA.
AC   B2HEN2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=MMAR_1281;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(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; CP000854; ACC39739.1; -; Genomic_DNA.
DR   RefSeq; WP_012393152.1; NC_010612.1.
DR   AlphaFoldDB; B2HEN2; -.
DR   SMR; B2HEN2; -.
DR   STRING; 216594.MMAR_1281; -.
DR   EnsemblBacteria; ACC39739; ACC39739; MMAR_1281.
DR   KEGG; mmi:MMAR_1281; -.
DR   eggNOG; COG0391; Bacteria.
DR   HOGENOM; CLU_055795_0_0_11; -.
DR   OMA; DLDTVMY; -.
DR   OrthoDB; 1079756at2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001190; 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; Reference proteome; Transferase.
FT   CHAIN           1..329
FT                   /note="Phosphoenolpyruvate transferase"
FT                   /id="PRO_1000139981"
FT   BINDING         61
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   329 AA;  35393 MW;  28720317616C95A3 CRC64;
     MKLTVLVGGV GGARFLLGAQ RLLGLGQFAT PDDNARHELT AVVNIGDDAW IHGLRICPDL
     DTCMYTLGGG VDPQRGWGHR DETWHAKEEL ARYGVQPDWF QLGDRDLATH LVRTQMLRAG
     YPLAQITTAL CDRWQPGATL LPVSNDRCET HVVVTDPTDQ QQRAIHFQEW WVRYRAELPT
     HSFVFIGTET ASATTEVTAA IADADVVMLA PSNPVVSIGA ILAVPGIRAA LRATRAPIIG
     YSPIIAGKPV RGMADACLSV IGVDTTAEAV GRHYGARAAT GVLDYWLVAE GDQAEIDSVT
     VRSIPLLMSD PEATAQMVRA GLELAGVTV