COFE_METTH
ID COFE_METTH Reviewed; 252 AA.
AC O27098;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01258};
DE EC=6.3.2.31 {ECO:0000255|HAMAP-Rule:MF_01258};
DE EC=6.3.2.34 {ECO:0000255|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01258};
GN Name=cofE {ECO:0000255|HAMAP-Rule:MF_01258}; OrderedLocusNames=MTH_1019;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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 {ECO:0000255|HAMAP-Rule:MF_01258}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01258};
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01258};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01258};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01258};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000255|HAMAP-Rule:MF_01258};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01258};
CC Note=Monovalent cation. The ion could be potassium. {ECO:0000255|HAMAP-
CC Rule:MF_01258};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01258}.
CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000255|HAMAP-
CC Rule:MF_01258}.
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DR EMBL; AE000666; AAB85515.1; -; Genomic_DNA.
DR PIR; H69002; H69002.
DR RefSeq; WP_010876650.1; NC_000916.1.
DR AlphaFoldDB; O27098; -.
DR SMR; O27098; -.
DR STRING; 187420.MTH_1019; -.
DR EnsemblBacteria; AAB85515; AAB85515; MTH_1019.
DR GeneID; 1471427; -.
DR KEGG; mth:MTH_1019; -.
DR PATRIC; fig|187420.15.peg.1002; -.
DR HOGENOM; CLU_051152_1_1_2; -.
DR OMA; KHGFVCA; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01258; F420_ligase_CofE; 1.
DR InterPro; IPR008225; F420-0_g-glutamyl_ligase.
DR InterPro; IPR002847; F420-0_gamma-glut_ligase-dom.
DR InterPro; IPR023659; F420_ligase_CofE_arc.
DR Pfam; PF01996; F420_ligase; 1.
DR TIGRFAMs; TIGR01916; F420_cofE; 1.
PE 3: Inferred from homology;
KW GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome.
FT CHAIN 1..252
FT /note="Coenzyme F420:L-glutamate ligase"
FT /id="PRO_0000145793"
FT BINDING 11..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 45..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 115
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 157
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 212..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
SQ SEQUENCE 252 AA; 26538 MW; ED65D0C08A479BA7 CRC64;
MGISLIGVEG MPLVGAGDDI AYLIISALNE GGEDLLDGDI IVIAETIVSK AEGNIISLEE
IKPSPEALDI AERTGKDPSL VEAILGESSE IIRVGHDFIV SETRHGFVCA NAGIDESNVD
DGLATPLPRD PDGSAEKILR TLQEATGREL AVIISDTQGR PFREGAVGVA VGVAGLSPIW
DRKGERDLYG RSLETTRVAV ADELAAAASL VMGQADEGVP AVIIRGYPWG HLRSDGGVKP
LLRPRELDVF RG
