AC MF_01259; DC Protein; auto TR HAMAP; MF_01259; -; 1; level=0 XX Names: F420_ligase_FbiB XX ID FBIB DE RecName: Full=Bifunctional F420 biosynthesis protein FbiB; DE Includes: DE RecName: Full=Coenzyme F420:L-glutamate ligase; DE EC=6.3.2.31; DE EC=6.3.2.34; DE AltName: Full=Coenzyme F420-0:L-glutamate ligase; DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase; DE Includes: DE RecName: Full=Dehydro-coenzyme F420-0 reductase; DE EC=1.3.8.17; GN Name=fbiB; XX case CC -!- FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent CC successive addition of multiple gamma-linked L-glutamates to the L- CC lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin CC (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- CC dependent reduction of dehydro-F420-0 to form F420-0. else CC -!- FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent CC successive addition of two or more gamma-linked L-glutamates to the L- CC lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin CC (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- CC dependent reduction of dehydro-F420-0 to form F420-0. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + CC oxidized coenzyme F420-1 + phosphate; Xref=Rhea:RHEA:30555, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:59907, CC ChEBI:CHEBI:59920; EC=6.3.2.31; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + CC oxidized coenzyme F420-2 + phosphate; Xref=Rhea:RHEA:30523, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57922, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:59920; EC=6.3.2.34; case CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + L-glutamate + oxidized coenzyme F420-(gamma-L-Glu)(n) = CC GDP + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n+1) + phosphate; CC Xref=Rhea:RHEA:51236, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:12940, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:133980; end case CC -!- CATALYTIC ACTIVITY: CC Reaction=FMN + H(+) + oxidized coenzyme F420-0 = dehydro coenzyme F420- CC 0 + FMNH2; Xref=Rhea:RHEA:60360, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59907, CC ChEBI:CHEBI:143705; EC=1.3.8.17; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 2 divalent metal cations per subunit. The ions could be CC magnesium and/or manganese.; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Note=Monovalent cation. The ion could be potassium.; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SIMILARITY: In the N-terminal section; belongs to the CofE family. XX DR Pfam; PF01996; F420_ligase; 1; trigger=no DR Pfam; PF00881; Nitroreductase; 1; trigger=no DR NCBIfam; TIGR01916; F420_cofE; 1; trigger=no DR NCBIfam; TIGR03553; F420_FbiB_CTERM; 1; trigger=no XX KW GTP-binding KW Ligase KW Magnesium KW Manganese KW Metal-binding KW Multifunctional enzyme KW Nucleotide-binding KW Oxidoreductase KW Potassium XX GO GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity GO GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity GO GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor GO GO:0052645; P:F420-0 metabolic process XX FT From: FBIB_MYCBO (Q7TWV3) FT BINDING 20..23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: [LIMV]-P-x-[IVEF] FT BINDING 260..264 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: R-x-S-x-R FT REGION Nter..244 FT /note="Coenzyme F420:L-glutamate ligase" FT REGION 245..Cter FT /note="Dehydro-coenzyme F420-0 reductase" FT BINDING 109 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: D FT BINDING 150 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: D FT BINDING 151 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT Condition: [TS] FT BINDING 50 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: S FT BINDING 55 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: K FT BINDING 112 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Condition: N FT BINDING 288 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: A FT BINDING 320 FT /ligand="coenzyme F420-(gamma-Glu)n" FT /ligand_id="ChEBI:CHEBI:133980" FT Condition: D FT BINDING 399 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: [GS] FT BINDING 436 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: R XX Size: 423-457; Related: MF_01258; Template: P9WP79; Q7TWV3; A0QTG1; Scope: Bacteria; Mycobacterium Bacteria; Nocardia Bacteria; Streptomyces Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: CofE homologs are found in the genomes of all organisms currently known to produce coenzyme F420. These include not only the methanogenic archaea but also nonmethanogenic archaea such as Halobacteria and Archaeoglobus (see MF_01258), as well as some eubacteria such as Streptomyces, Mycobacterium, Nocardia, and Thermobifida (this rule, MF_01259). The length of the polyglutamate tail varies in different organisms. According to PubMed:12867481 (Graupner et al., 2003) and PubMed:11479701 (Bair et al., 2001): Analyses of the F420s present in Methanococcus jannaschii have shown that these cells contain a series of gamma-glutamyl-linked F420s capped with a single, terminal alpha-linked L-glutamate. The predominant form of F420 was designated as alpha-F420-3 and represented 86% of the F420s in these cells. Analyses of Methanosarcina thermophila, Methanosarcina barkeri, Methanobacterium thermoautotrophicum, Archaeoglobus fulgidus, and Mycobacterium smegmatis showed that they contained only gamma-glutamyl-linked F420s, with the following predominant forms: Methanosarcina thermophila (gamma-F420-3, 19%; gamma-F420-4, 62%), Methanosarcina barkeri (gamma-F420-2, 31%; gamma-F420-4, 32%), Methanobacterium thermoautotrophicum (gamma-F420-2, 80%), Archaeoglobus fulgidus (gamma-F420-4, 89%), and Mycobacterium smegmatis (gamma-F420-5, 67%; gamma-F420-6, 31%). In mycobacteria, the length of the polyglutamate tail varies by up to nine residues, with predominant species containing four to seven glutamate molecules (Bair et al., 2001, PubMed:11479701; Bashiri et al., 2008, PubMed:18434308). XX # Revision 1.27 2023/06/01 //