AC   MF_01258;
DC   Protein; auto
TR   HAMAP; MF_01258; -; 1; level=0
XX
Names: F420_ligase_CofE
XX
ID   COFE
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;
GN   Name=cofE;
XX
CC   -!- FUNCTION: Catalyzes the GTP-dependent successive addition of two or
CC       more gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-
CC       didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-
CC       0-glutamyl-glutamate (F420-2) or polyglutamated F420 derivatives.
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;
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   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the CofE family.
XX
DR   Pfam; PF01996; F420_ligase; 1; trigger=no
DR   NCBIfam; TIGR01916; F420_cofE; 1; trigger=no
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KW   GTP-binding
KW   Ligase
KW   Magnesium
KW   Manganese
KW   Metal-binding
KW   Nucleotide-binding
KW   Potassium
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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:0052645; P:F420-0 metabolic process
XX
FT   From: COFE_ARCFU (O28028)
FT   BINDING         11..14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: [LIMV]-P-x-[IVEF]
FT   BINDING         40..41
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: [SEH]-T
FT   BINDING         206..213
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
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         208
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT   Condition: [EQ]
FT   BINDING         45
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
XX
Size: 248-257;
Related: MF_01259!;
Template: Q58178; O28028;
Scope:
 Archaea; Archaeoglobi
 Archaea; Halobacteria
 Archaea; Methanobacteria
 Archaea; Methanococci
 Archaea; Methanomicrobia
 Archaea; Methanopyri
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, as well
 as some eubacteria such as Streptomyces, Mycobacterium, Nocardia, and
 Thermobifida (see 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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# Revision 1.21 2023/06/01
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