ID F2KRL8_ARCVS Unreviewed; 258 AA.
AC F2KRL8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
DE EC=6.3.2.31 {ECO:0000256|HAMAP-Rule:MF_01258};
DE EC=6.3.2.34 {ECO:0000256|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
GN Name=cofE {ECO:0000256|HAMAP-Rule:MF_01258};
GN OrderedLocusNames=Arcve_0767 {ECO:0000313|EMBL:AEA46783.1};
OS Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA46783.1, ECO:0000313|Proteomes:UP000008136};
RN [1] {ECO:0000313|EMBL:AEA46783.1, ECO:0000313|Proteomes:UP000008136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNP6;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Archaeoglobus veneficus SNP6.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01258};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
CC Note=Monovalent cation. The ion could be potassium. {ECO:0000256|HAMAP-
CC Rule:MF_01258};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000256|HAMAP-Rule:MF_01258};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01258}.
CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000256|HAMAP-
CC Rule:MF_01258}.
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DR EMBL; CP002588; AEA46783.1; -; Genomic_DNA.
DR RefSeq; WP_013683455.1; NC_015320.1.
DR AlphaFoldDB; F2KRL8; -.
DR STRING; 693661.Arcve_0767; -.
DR GeneID; 10393870; -.
DR KEGG; ave:Arcve_0767; -.
DR eggNOG; arCOG02714; Archaea.
DR HOGENOM; CLU_051152_1_1_2; -.
DR OrthoDB; 11383at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000008136; 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 Gene3D; 3.30.1330.100; CofE-like; 1.
DR Gene3D; 3.90.1660.10; CofE-like domain; 1.
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 NCBIfam; TIGR01916; F420_cofE; 1.
DR PANTHER; PTHR47917; -; 1.
DR PANTHER; PTHR47917:SF1; COENZYME F420:L-GLUTAMATE LIGASE; 1.
DR Pfam; PF01996; F420_ligase; 1.
DR SUPFAM; SSF144010; CofE-like; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01258};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01258};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01258};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01258};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01258};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01258};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01258};
KW Reference proteome {ECO:0000313|Proteomes:UP000008136}.
FT DOMAIN 8..220
FT /note="Coenzyme F420:L-glutamate ligase-like"
FT /evidence="ECO:0000259|Pfam:PF01996"
FT BINDING 11..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 41..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 110
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 113
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 206..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 208
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
SQ SEQUENCE 258 AA; 28417 MW; 33B2A847B8F1E06E CRC64;
MHEVRVTGIK LPIIRANSGI ASLAALIAPY VESGDVVAIC STIVSKAEGR LRRLEEYTPC
EKAIKIAERL CEDPRLVQAV LEESEEVLID YPFLLVKAKF GNVCVNAGID RSNVEPGFIL
LPPENPDRSA ERIREELVKT GKDVGIIITD TNGRCFRKGV TGFAIGVSGV VPLRDWKGKK
DLYGNDLQRT EECIADEIAA FANLIMGEGD SGIPAVVFRG LKFWLGEDDD IDEGMKAVYR
SEAEDVIRRL IKLARSEK
//
