COFE_ARCFU
ID COFE_ARCFU Reviewed; 249 AA.
AC O28028;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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;
DE AltName: Full=F420:glutamyl ligase;
GN Name=cofE; OrderedLocusNames=AF_2256;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH GDP
RP AND MN(2+), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=17669425; DOI=10.1016/j.jmb.2007.06.063;
RA Nocek B., Evdokimova E., Proudfoot M., Kudritska M., Grochowski L.L.,
RA White R.H., Savchenko A., Yakunin A.F., Edwards A., Joachimiak A.;
RT "Structure of an amide bond forming F(420):gamma-glutamyl ligase from
RT Archaeoglobus fulgidus -- a member of a new family of non-ribosomal peptide
RT synthases.";
RL J. Mol. Biol. 372:456-469(2007).
CC -!- FUNCTION: Catalyzes the GTP-dependent successive addition of two L-
CC glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-
CC 5-deazariboflavin (F420-0) to form coenzyme F420-0-glutamyl-glutamate
CC (F420-2), with a gamma-linkage between the two glutamates. May be able
CC to add up to four gamma-linked glutamates, since F420-4 is a species
CC that was isolated from A.fulgidus. {ECO:0000269|PubMed:17669425}.
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 Evidence={ECO:0000269|PubMed:17669425};
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 Evidence={ECO:0000269|PubMed:17669425};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17669425};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17669425};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000269|PubMed:17669425};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC Note=Monovalent cation. The ion could be potassium. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17669425}.
CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB89001.1; -; Genomic_DNA.
DR PIR; H69531; H69531.
DR RefSeq; WP_010879745.1; NC_000917.1.
DR PDB; 2G9I; X-ray; 2.50 A; A/B=1-249.
DR PDB; 2PHN; X-ray; 1.35 A; A/B=1-249.
DR PDBsum; 2G9I; -.
DR PDBsum; 2PHN; -.
DR AlphaFoldDB; O28028; -.
DR SMR; O28028; -.
DR STRING; 224325.AF_2256; -.
DR EnsemblBacteria; AAB89001; AAB89001; AF_2256.
DR GeneID; 24796019; -.
DR KEGG; afu:AF_2256; -.
DR eggNOG; arCOG02714; Archaea.
DR HOGENOM; CLU_051152_1_1_2; -.
DR OMA; KHGFVCA; -.
DR OrthoDB; 73785at2157; -.
DR PhylomeDB; O28028; -.
DR BRENDA; 6.3.2.31; 11304.
DR BRENDA; 6.3.2.34; 11304.
DR UniPathway; UPA00071; -.
DR EvolutionaryTrace; O28028; -.
DR Proteomes; UP000002199; 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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome.
FT CHAIN 1..249
FT /note="Coenzyme F420:L-glutamate ligase"
FT /id="PRO_0000145785"
FT BINDING 11..14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 40..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 45
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 BINDING 112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT BINDING 206..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 208
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 157..170
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2G9I"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2G9I"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2PHN"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2PHN"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2PHN"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:2PHN"
SQ SEQUENCE 249 AA; 27261 MW; EC64A6D40FDD8B97 CRC64;
MRVEVFPVEG LPLIKEGDDL AELISSRVRF EDGDVLVVCS TVISKAEGRI RRLEEFNPSE
RAKEIAARIG KPAEFVQAVL EESEEVLLDF PFLLVKAKFG NVCVNAGIDA SNVEEGSLLL
PPLDPDGSAE KLRRRILELT GKRVGVIITD TNGRCFRRGV VGFAIGISGV KAMKDWIGRK
DLYGRELEVT VECVADEIAA FANLLMGEGG DGIPAVVVRG LNVAGEGSME EIYRSEEEDV
IRRCLKRCL
