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HAMAP rule MF_01259

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General rule information [?]

Accession MF_01259
Dates 21-APR-2005 (Created)
1-JUN-2023 (Last updated, Version 27)
Name F420_ligase_FbiB
Scope(s) Bacteria
Mycobacterium
Nocardia
Streptomyces
Template(s) P9WP79 (FBIB_MYCTU); Q7TWV3 (FBIB_MYCBO); A0QTG1 (FBIB_MYCS2); [ Recover all ]
Triggered by HAMAP; MF_01259 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier FBIB
Protein name RecName: Full=Bifunctional F420 biosynthesis protein FbiB;
                 Includes:
RecName: Full=Coenzyme F420:L-glutamate ligase;
                 EC=6.3.2.31;
                 EC=6.3.2.34;
AltName: Full=Coenzyme F420-0:L-glutamate ligase;
AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase;
                 Includes:
RecName: Full=Dehydro-coenzyme F420-0 reductase;
                 EC=1.3.8.17;
Gene name Name=fbiB;

Comments [?]

case <OC:Mycobacterium>
FUNCTIONBifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0.
else
FUNCTIONBifunctional enzyme that catalyzes the GTP-dependent successive addition of two or more gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0.
end case
CATALYTIC ACTIVITY Reaction=GTP + L-glutamate + oxidized coenzyme F420-0 = GDP + H(+) + oxidized coenzyme F420-1 + phosphate; Xref=Rhea:RHEA:30555, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:59907, ChEBI:CHEBI:59920; EC=6.3.2.31;
CATALYTIC ACTIVITY Reaction=GTP + L-glutamate + oxidized coenzyme F420-1 = GDP + H(+) + oxidized coenzyme F420-2 + phosphate; Xref=Rhea:RHEA:30523, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57922, ChEBI:CHEBI:58189, ChEBI:CHEBI:59920; EC=6.3.2.34;
case <OC:Mycobacterium>
CATALYTIC ACTIVITY Reaction=GTP + L-glutamate + oxidized coenzyme F420-(gamma-L-Glu)(n) = GDP + H(+) + oxidized coenzyme F420-(gamma-L-Glu)(n+1) + phosphate; Xref=Rhea:RHEA:51236, Rhea:RHEA-COMP:12939, Rhea:RHEA-COMP:12940, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:133980;
end case
CATALYTIC ACTIVITY Reaction=FMN + H(+) + oxidized coenzyme F420-0 = dehydro coenzyme F420- 0 + FMNH2; Xref=Rhea:RHEA:60360, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59907, ChEBI:CHEBI:143705; EC=1.3.8.17;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.;
COFACTOR Name=K(+); Xref=ChEBI:CHEBI:29103; Note=Monovalent cation. The ion could be potassium.;
PATHWAYCofactor biosynthesis; coenzyme F420 biosynthesis.
SIMILARITYIn the N-terminal section; belongs to the CofE family.

Keywords [?]


Gene Ontology [?]

GO:0052618; Molecular function:coenzyme F420-0:L-glutamate ligase activity
GO:0052619; Molecular function:coenzyme F420-1:gamma-L-glutamate ligase activity
GO:0052890; Molecular function:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor
GO:0052645; Biological process:F420-0 metabolic process

Cross-references [?]

Pfam PF01996; F420_ligase; 1;
Pfam PF00881; Nitroreductase; 1;
NCBIfam TIGR01916; F420_cofE; 1;
NCBIfam TIGR03553; F420_FbiB_CTERM; 1;

Features [?]

From: FBIB_MYCBO (Q7TWV3)
Key From To Description Tag Condition FTGroup
BINDING 20 23 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
[LIMV]-P-x-[IVEF]
BINDING 260 264 /ligand="FMN"
/ligand_id="ChEBI:CHEBI:58210"
R-x-S-x-R
REGION Nter 244 /note="Coenzyme F420:L-glutamate ligase"
REGION 245 Cter /note="Dehydro-coenzyme F420-0 reductase"
BINDING 109 109 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="1"
D
BINDING 150 150 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="1"
D
BINDING 151 151 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"
/ligand_label="2"
[TS]
BINDING 50 50 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
S
BINDING 55 55 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
K
BINDING 112 112 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
N
BINDING 288 288 /ligand="FMN"
/ligand_id="ChEBI:CHEBI:58210"
A
BINDING 320 320 /ligand="coenzyme F420-(gamma-Glu)n"
/ligand_id="ChEBI:CHEBI:133980"
D
BINDING 399 399 /ligand="FMN"
/ligand_id="ChEBI:CHEBI:58210"
[GS]
BINDING 436 436 /ligand="FMN"
/ligand_id="ChEBI:CHEBI:58210"
R

Additional information [?]

Size range 423-457 amino acids
Related rules MF_01258
Fusion Nter: None Cter: 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).



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