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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_METJA              Reviewed;         249 AA.
Q58178;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 97.
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=MJ0768;
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 /
JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
Archaea; Euryarchaeota; Methanococci; Methanococcales;
Methanocaldococcaceae; Methanocaldococcus.
NCBI_TaxID=243232;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=8688087; DOI=10.1126/science.273.5278.1058;
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D.,
Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
"Complete genome sequence of the methanogenic archaeon, Methanococcus
jannaschii.";
Science 273:1058-1073(1996).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM.
STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
PubMed=12911320; DOI=10.1021/bi034779b;
Li H., Graupner M., Xu H., White R.H.;
"CofE catalyzes the addition of two glutamates to F420-0 in F420
coenzyme biosynthesis in Methanococcus jannaschii.";
Biochemistry 42:9771-9778(2003).
-!- 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. Cannot use F420-2 as substrate to add more glutamates.
Exhibits maximum activity with GTP, compared with UTP (66%) and
dGTP (25%); with ATP, only F420-1 is observed as the product; CTP
and TTP support no activity. {ECO:0000269|PubMed:12911320}.
-!- CATALYTIC ACTIVITY: GTP + coenzyme F420-0 + L-glutamate = GDP +
phosphate + coenzyme F420-1. {ECO:0000269|PubMed:12911320}.
-!- CATALYTIC ACTIVITY: GTP + coenzyme F420-1 + L-glutamate = GDP +
phosphate + coenzyme gamma-F420-2. {ECO:0000269|PubMed:12911320}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12911320};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:12911320};
Note=Binds 2 divalent metal cations per subunit. The ions could be
magnesium and/or manganese. {ECO:0000269|PubMed:12911320};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000269|PubMed:12911320};
Note=Monovalent cation. The ion could be potassium.
{ECO:0000269|PubMed:12911320};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.0 uM for F420-0 {ECO:0000269|PubMed:12911320};
KM=0.21 uM for F420-1 {ECO:0000269|PubMed:12911320};
Vmax=2.4 nmol/min/mg enzyme with F420-0 as substrate
{ECO:0000269|PubMed:12911320};
Vmax=0.96 nmol/min/mg enzyme with F420-1 as substrate
{ECO:0000269|PubMed:12911320};
pH dependence:
Optimum pH is 8.5. {ECO:0000269|PubMed:12911320};
Temperature dependence:
Optimum temperature is 60 degrees Celsius. Thermostable. Retains
70% of its activity after heating at 80 degrees Celsius for 15
minutes. {ECO:0000269|PubMed:12911320};
-!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12911320}.
-!- SIMILARITY: Belongs to the CofE family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L77117; AAB98763.1; -; Genomic_DNA.
PIR; H64395; H64395.
RefSeq; WP_010870273.1; NC_000909.1.
ProteinModelPortal; Q58178; -.
SMR; Q58178; -.
STRING; 243232.MJ_0768; -.
EnsemblBacteria; AAB98763; AAB98763; MJ_0768.
GeneID; 1451645; -.
KEGG; mja:MJ_0768; -.
eggNOG; arCOG02714; Archaea.
eggNOG; COG1478; LUCA.
InParanoid; Q58178; -.
KO; K12234; -.
OMA; GFVCANS; -.
OrthoDB; POG093Z0KDL; -.
PhylomeDB; Q58178; -.
BioCyc; MetaCyc:MONOMER-12187; -.
BRENDA; 6.3.2.31; 3260.
BRENDA; 6.3.2.34; 3260.
SABIO-RK; Q58178; -.
UniPathway; UPA00071; -.
Proteomes; UP000000805; 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; IDA:MENGO.
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;
Complete proteome; GTP-binding; Ligase; Magnesium; Manganese;
Metal-binding; Nucleotide-binding; Potassium; Reference proteome.
CHAIN 1 249 Coenzyme F420:L-glutamate ligase.
/FTId=PRO_0000145789.
NP_BIND 15 18 GTP. {ECO:0000250}.
NP_BIND 45 46 GTP. {ECO:0000250}.
NP_BIND 211 218 GTP. {ECO:0000250}.
METAL 115 115 Divalent metal cation 1. {ECO:0000250}.
METAL 155 155 Divalent metal cation 1. {ECO:0000250}.
METAL 156 156 Divalent metal cation 2. {ECO:0000250}.
METAL 213 213 Divalent metal cation 2. {ECO:0000250}.
BINDING 50 50 GTP. {ECO:0000250}.
BINDING 118 118 GTP. {ECO:0000250}.
SEQUENCE 249 AA; 27148 MW; A6B66FF4B52C15A2 CRC64;
MIKEKRKVEV IGLELPIFKG GEQINLSELI AQYPIEDGDI IVIAETLISK LEGGVIDRDK
IIPSKEAIEL AKKTGKDPKV VQVILDEAKE IVKVGKNFII TETKHGFVCA NSGVDESNIY
KGIKILPKNP DESAEKIRKE IEKLTGKRVG VIISDSVGRP FRKGAVGIAI GVSGILALWD
RKGEKDLFGR ELKTTEVAIA DELASMANVV MGEADEGIPV VIIRGANVPF GNGKGRDLIR
PKEEDVFRN


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