HAMAP rule MF_01259
General rule information
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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
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Identifier, protein and gene names
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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
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case <OC:Mycobacterium> | |
FUNCTION | Bifunctional 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 | |
FUNCTION | Bifunctional 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.; |
PATHWAY | Cofactor biosynthesis; coenzyme F420 biosynthesis. |
SIMILARITY | In the N-terminal section; belongs to the CofE family. |
Keywords
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GTP-binding |
Ligase |
Magnesium |
Manganese |
Metal-binding |
Multifunctional enzyme |
Nucleotide-binding |
Oxidoreductase |
Potassium |
Gene Ontology
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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
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Pfam | PF01996; F420_ligase; 1; |
Pfam | PF00881; Nitroreductase; 1; |
NCBIfam | TIGR01916; F420_cofE; 1; |
NCBIfam | TIGR03553; F420_FbiB_CTERM; 1; |
Features
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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
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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). |