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Coenzyme F420:L-glutamate ligase (EC 6.3.2.31) (EC 6.3.2.34) (Coenzyme F420-0:L-glutamate ligase) (Coenzyme F420-1:gamma-L-glutamate ligase) (F420:glutamyl ligase)

 COFE_ARCFU              Reviewed;         249 AA.
O28028;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
07-JUN-2017, entry version 95.
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;
AltName: Full=F420:glutamyl ligase;
Name=cofE; OrderedLocusNames=AF_2256;
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
9628 / NBRC 100126).
Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
Archaeoglobaceae; Archaeoglobus.
NCBI_TaxID=224325;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
PubMed=9389475; DOI=10.1038/37052;
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
Woese C.R., Venter J.C.;
"The complete genome sequence of the hyperthermophilic, sulphate-
reducing archaeon Archaeoglobus fulgidus.";
Nature 390:364-370(1997).
[2]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH GDP AND MN(2+), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
SUBUNIT.
STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
PubMed=17669425; DOI=10.1016/j.jmb.2007.06.063;
Nocek B., Evdokimova E., Proudfoot M., Kudritska M., Grochowski L.L.,
White R.H., Savchenko A., Yakunin A.F., Edwards A., Joachimiak A.;
"Structure of an amide bond forming F(420):gamma-glutamyl ligase from
Archaeoglobus fulgidus -- a member of a new family of non-ribosomal
peptide synthases.";
J. Mol. Biol. 372:456-469(2007).
-!- FUNCTION: Catalyzes the GTP-dependent successive addition of two
L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-
hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0-
glutamyl-glutamate (F420-2), with a gamma-linkage between the two
glutamates. May be able to add up to four gamma-linked glutamates,
since F420-4 is a species that was isolated from A.fulgidus.
{ECO:0000269|PubMed:17669425}.
-!- CATALYTIC ACTIVITY: GTP + coenzyme F420-0 + L-glutamate = GDP +
phosphate + coenzyme F420-1. {ECO:0000269|PubMed:17669425}.
-!- CATALYTIC ACTIVITY: GTP + coenzyme F420-1 + L-glutamate = GDP +
phosphate + coenzyme gamma-F420-2. {ECO:0000269|PubMed:17669425}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17669425};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17669425};
Note=Binds 2 divalent metal cations per subunit. The ions could be
magnesium and/or manganese. {ECO:0000269|PubMed:17669425};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
Note=Monovalent cation. The ion could be potassium. {ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17669425}.
-!- SIMILARITY: Belongs to the CofE family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE000782; AAB89001.1; -; Genomic_DNA.
PIR; H69531; H69531.
RefSeq; WP_010879745.1; NC_000917.1.
PDB; 2G9I; X-ray; 2.50 A; A/B=1-249.
PDB; 2PHN; X-ray; 1.35 A; A/B=1-249.
PDBsum; 2G9I; -.
PDBsum; 2PHN; -.
ProteinModelPortal; O28028; -.
SMR; O28028; -.
STRING; 224325.AF2256; -.
EnsemblBacteria; AAB89001; AAB89001; AF_2256.
GeneID; 24796019; -.
KEGG; afu:AF_2256; -.
eggNOG; arCOG02714; Archaea.
eggNOG; COG1478; LUCA.
KO; K12234; -.
OMA; GFVCANS; -.
OrthoDB; POG093Z0KDL; -.
BRENDA; 6.3.2.31; 11304.
BRENDA; 6.3.2.34; 11304.
UniPathway; UPA00071; -.
EvolutionaryTrace; O28028; -.
Proteomes; UP000002199; Chromosome.
GO; GO:0043773; F:coenzyme F420-0 gamma-glutamyl ligase activity; IEA:InterPro.
GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IEA:UniProtKB-EC.
GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-EC.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051188; P:cofactor biosynthetic process; IEA:InterPro.
HAMAP; MF_01258; F420_ligase_CofE; 1.
InterPro; IPR008225; F420-0_g-glutamyl_ligase.
InterPro; IPR002847; F420-0_gamma-glut_ligase-dom.
InterPro; IPR023659; F420_ligase_CofE_arc.
Pfam; PF01996; F420_ligase; 1.
TIGRFAMs; TIGR01916; F420_cofE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; GTP-binding; Ligase; Magnesium;
Manganese; Metal-binding; Nucleotide-binding; Potassium;
Reference proteome.
CHAIN 1 249 Coenzyme F420:L-glutamate ligase.
/FTId=PRO_0000145785.
NP_BIND 11 14 GTP.
NP_BIND 40 41 GTP.
NP_BIND 206 213 GTP.
METAL 109 109 Divalent metal cation 1.
METAL 150 150 Divalent metal cation 1.
METAL 151 151 Divalent metal cation 2.
METAL 208 208 Divalent metal cation 2.
BINDING 45 45 GTP.
BINDING 112 112 GTP.
STRAND 3 7 {ECO:0000244|PDB:2PHN}.
HELIX 20 25 {ECO:0000244|PDB:2PHN}.
STRAND 35 39 {ECO:0000244|PDB:2PHN}.
HELIX 40 46 {ECO:0000244|PDB:2PHN}.
STRAND 50 52 {ECO:0000244|PDB:2PHN}.
HELIX 53 55 {ECO:0000244|PDB:2PHN}.
HELIX 60 69 {ECO:0000244|PDB:2PHN}.
HELIX 73 81 {ECO:0000244|PDB:2PHN}.
STRAND 83 88 {ECO:0000244|PDB:2PHN}.
STRAND 90 92 {ECO:0000244|PDB:2PHN}.
STRAND 94 97 {ECO:0000244|PDB:2PHN}.
STRAND 102 104 {ECO:0000244|PDB:2PHN}.
HELIX 105 107 {ECO:0000244|PDB:2PHN}.
STRAND 111 113 {ECO:0000244|PDB:2PHN}.
STRAND 117 119 {ECO:0000244|PDB:2PHN}.
HELIX 125 140 {ECO:0000244|PDB:2PHN}.
STRAND 145 154 {ECO:0000244|PDB:2PHN}.
STRAND 157 170 {ECO:0000244|PDB:2PHN}.
STRAND 172 175 {ECO:0000244|PDB:2G9I}.
STRAND 191 193 {ECO:0000244|PDB:2G9I}.
HELIX 194 206 {ECO:0000244|PDB:2PHN}.
STRAND 208 211 {ECO:0000244|PDB:2PHN}.
STRAND 215 220 {ECO:0000244|PDB:2PHN}.
HELIX 229 231 {ECO:0000244|PDB:2PHN}.
TURN 236 238 {ECO:0000244|PDB:2PHN}.
HELIX 240 248 {ECO:0000244|PDB:2PHN}.
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


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