FBIA_THEFY
ID FBIA_THEFY Reviewed; 322 AA.
AC Q47LX2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
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=Tfu_2517;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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=AAZ56550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000088; AAZ56550.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_016189180.1; NC_007333.1.
DR AlphaFoldDB; Q47LX2; -.
DR SMR; Q47LX2; -.
DR STRING; 269800.Tfu_2517; -.
DR EnsemblBacteria; AAZ56550; AAZ56550; Tfu_2517.
DR KEGG; tfu:Tfu_2517; -.
DR eggNOG; COG0391; Bacteria.
DR HOGENOM; CLU_055795_0_0_11; -.
DR OrthoDB; 1079756at2; -.
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..322
FT /note="Phosphoenolpyruvate transferase"
FT /id="PRO_0000259477"
FT BINDING 58
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 322 AA; 34335 MW; 3C7A1279B254C6CE CRC64;
MRIVVLAGGI GGARFLRGLK DALHHRAEQG ESPSSITVIG NTGDDITLFG LRVCPDLDTV
MYTLGGGINE EQGWGRADET FTVREELIAY GMHPQWFGLG DRDIATHIVR SQMLAAGYPL
SAITEALCDR WKPGVRLLPM TDDQVETHVV VADEKGRRAI HFQEWWVRYR AQIPAESFVS
VGADSAKPAP GVLSAIDEAD FVLFPPSNPV VSIGSILGIP GIRDAVAAKT VVGVSPIIGG
APVRGMADAC LRTIGVETSA RAVAEHYGAD LLDGWLVDEA DADTVVAGVE VRAMPLYMSD
PERTAAIAGA AVDLALELKE RS
