ID   FBIA_MYCSJ              Reviewed;         331 AA.
AC   A3PW85;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=Mjls_1360;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000580; ABN97162.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3PW85; -.
DR   SMR; A3PW85; -.
DR   STRING; 164757.Mjls_1360; -.
DR   KEGG; mjl:Mjls_1360; -.
DR   HOGENOM; CLU_055795_0_0_11; -.
DR   OMA; DLDTVMY; -.
DR   BioCyc; MSP164757:G1G8C-1373-MON; -.
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   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_1000067252"
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;  35338 MW;  6241830A7CC61862 CRC64;
     MKVTVLVGGV GGARFLLGVQ HLLGLGQFAR DDARDPDAHE VTAVVNVGDD TWMFGVRICP
     DLDTCMYTLG GGIDPDRGWG HRDETWHAKE ELAAYGVQPD WFGLGDRDLA THLVRSQMLR
     AGYPLSQVTE ALCDRWNPGA RLLPASDDRS ETHVVITDPD TDERRAIHFQ EWWVRYRAKV
     PTHSFAFVGA DKATTAPGVT DAIADADVVL LAPSNPVVSI GSILAIPGIR GALRSTSAKI
     IGYSPIIAGK PLRGMADECL SVIGVASTSE AVGRHYGARS GTGILDGWLV HEGDSAQIDG
     VEVEAVPLLM TDPATTAEMV RAGVRLAGVT L