ID   FBIA_KITAU              Reviewed;         321 AA.
AC   Q75UN1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 60.
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}; ORFNames=tch-ORF2;
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Kitasatospora.
OX   NCBI_TaxID=1894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HP77;
RX   PubMed=15215601; DOI=10.1271/bbb.68.1345;
RA   Nakano T., Miyake K., Endo H., Dairi T., Mizukami T., Katsumata R.;
RT   "Identification and cloning of the gene involved in the final step of
RT   chlortetracycline biosynthesis in Streptomyces aureofaciens.";
RL   Biosci. Biotechnol. Biochem. 68:1345-1352(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD16616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB125899; BAD16616.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_030289941.1; NZ_LBHA01000399.1.
DR   AlphaFoldDB; Q75UN1; -.
DR   SMR; Q75UN1; -.
DR   STRING; 1894.JOER01000062_gene88; -.
DR   eggNOG; COG0391; Bacteria.
DR   OMA; DLDTVMY; -.
DR   UniPathway; UPA00071; -.
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   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..321
FT                   /note="Phosphoenolpyruvate transferase"
FT                   /id="PRO_0000145765"
FT   BINDING         51
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   321 AA;  33660 MW;  239BAF3B855F760F CRC64;
     MRIVALAGGI GGARFLRGLL AAVGPQDEIT VIGNTGDDIH LYGLKVCPDL DTVMYTLGGG
     IHEEQGWGRA DETWSIKAEM KEYGVGPEWF GLGDRDFATH LVRSQMLTAG YSLSQVTEAL
     CVRWNPGVRL LPMSDDRVET HVRITDEQGT RAVHFQEYWV RLHAAVDAEA IIPVGADTAK
     PAPGVLEAIA EADVILFPPS NPVVSIGTIL AVPGIREAVA AAPAPVVGLS PIIGGAPVRG
     MADKVLAAVG VEATAEAVAL NYGPDLIDGW LVDTADEHAV AAVEAAGIAC RAVPLLMTDV
     EATAEMARTA LALAEQVRHG S