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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)

 I3R661_HALMT            Unreviewed;       251 AA.
I3R661; M0IVI4;
05-SEP-2012, integrated into UniProtKB/TrEMBL.
03-SEP-2014, sequence version 2.
28-FEB-2018, entry version 40.
RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
EC=6.3.2.31 {ECO:0000256|HAMAP-Rule:MF_01258};
EC=6.3.2.34 {ECO:0000256|HAMAP-Rule:MF_01258};
AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
Name=cofE {ECO:0000256|HAMAP-Rule:MF_01258,
ECO:0000313|EMBL:AFK19721.2};
OrderedLocusNames=HFX_2029 {ECO:0000313|EMBL:AFK19721.2};
ORFNames=BM92_10890 {ECO:0000313|EMBL:AHZ23109.1},
C439_11923 {ECO:0000313|EMBL:EMA00043.1};
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK19721.2, ECO:0000313|Proteomes:UP000006469};
[1] {ECO:0000313|EMBL:AFK19721.2}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
PubMed=22247127; DOI=10.1128/AEM.07114-11;
Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
"Identification of the haloarchaeal phasin (PhaP) that functions in
polyhydroxyalkanoate accumulation and granule formation in Haloferax
mediterranei.";
Appl. Environ. Microbiol. 78:1946-1952(2012).
[2] {ECO:0000313|EMBL:AFK19721.2, ECO:0000313|Proteomes:UP000006469}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000006469}, and
CGMCC 1.2087 {ECO:0000313|EMBL:AFK19721.2};
PubMed=22843593; DOI=10.1128/JB.00880-12;
Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
Chen Y., Zhou J., Hu S., Xiang H.;
"Complete genome sequence of the metabolically versatile halophilic
archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
hydroxyvalerate) producer.";
J. Bacteriol. 194:4463-4464(2012).
[3] {ECO:0000313|Proteomes:UP000011603}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000011603};
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:EMA00043.1}
NUCLEOTIDE SEQUENCE.
STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA00043.1};
PubMed=25393412;
Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
"Phylogenetically driven sequencing of extremely halophilic archaea
reveals strategies for static and dynamic osmo-response.";
PLoS Genet. 10:E1004784-E1004784(2014).
[5] {ECO:0000313|EMBL:AHZ23109.1, ECO:0000313|Proteomes:UP000027075}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ23109.1}, and
ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
{ECO:0000313|Proteomes:UP000027075};
Bautista V.;
"Transcriptional profiles of Haloferax mediterranei on the basis of
nitrogen availability.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AFK19721.2}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
Wang L., Yang H., Xiang H.;
Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the GTP-dependent successive addition of two
or more gamma-linked 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) or polyglutamated F420
derivatives. {ECO:0000256|HAMAP-Rule:MF_01258}.
-!- CATALYTIC ACTIVITY: GTP + coenzyme F420-0 + L-glutamate = GDP +
phosphate + coenzyme F420-1. {ECO:0000256|HAMAP-Rule:MF_01258}.
-!- CATALYTIC ACTIVITY: GTP + coenzyme F420-1 + L-glutamate = GDP +
phosphate + coenzyme gamma-F420-2. {ECO:0000256|HAMAP-
Rule:MF_01258}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
Note=Monovalent cation. The ion could be potassium.
{ECO:0000256|HAMAP-Rule:MF_01258};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
Note=Binds 2 divalent metal cations per subunit. The ions could be
magnesium and/or manganese. {ECO:0000256|HAMAP-Rule:MF_01258};
-!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_01258}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01258}.
-!- SIMILARITY: Belongs to the CofE family. {ECO:0000256|HAMAP-
Rule:MF_01258}.
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EMBL; CP001868; AFK19721.2; -; Genomic_DNA.
EMBL; CP007551; AHZ23109.1; -; Genomic_DNA.
EMBL; AOLO01000009; EMA00043.1; -; Genomic_DNA.
RefSeq; WP_004059367.1; NZ_CP007551.1.
EnsemblBacteria; AFK19721; AFK19721; HFX_2029.
EnsemblBacteria; AHZ23109; AHZ23109; BM92_10890.
EnsemblBacteria; EMA00043; EMA00043; C439_11923.
GeneID; 13028189; -.
KEGG; hme:HFX_2029; -.
PATRIC; fig|523841.21.peg.2412; -.
KO; K12234; -.
OrthoDB; POG093Z0KDL; -.
BioCyc; HMED523841:G1HBL-2701-MONOMER; -.
UniPathway; UPA00071; -.
Proteomes; UP000006469; Chromosome.
Proteomes; UP000011603; Unassembled WGS sequence.
Proteomes; UP000027075; 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-UniRule.
GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009108; P:coenzyme biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
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.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000006469};
GTP-binding {ECO:0000256|HAMAP-Rule:MF_01258};
Ligase {ECO:0000256|HAMAP-Rule:MF_01258, ECO:0000313|EMBL:AFK19721.2};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01258};
Manganese {ECO:0000256|HAMAP-Rule:MF_01258};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01258};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01258};
Potassium {ECO:0000256|HAMAP-Rule:MF_01258};
Reference proteome {ECO:0000313|Proteomes:UP000006469}.
DOMAIN 9 219 F420_ligase. {ECO:0000259|Pfam:PF01996}.
NP_BIND 9 12 GTP. {ECO:0000256|HAMAP-Rule:MF_01258}.
NP_BIND 38 39 GTP. {ECO:0000256|HAMAP-Rule:MF_01258}.
NP_BIND 205 212 GTP. {ECO:0000256|HAMAP-Rule:MF_01258}.
METAL 113 113 Divalent metal cation 1.
{ECO:0000256|HAMAP-Rule:MF_01258}.
METAL 149 149 Divalent metal cation 1.
{ECO:0000256|HAMAP-Rule:MF_01258}.
METAL 150 150 Divalent metal cation 2.
{ECO:0000256|HAMAP-Rule:MF_01258}.
METAL 207 207 Divalent metal cation 2.
{ECO:0000256|HAMAP-Rule:MF_01258}.
BINDING 43 43 GTP. {ECO:0000256|HAMAP-Rule:MF_01258}.
BINDING 116 116 GTP. {ECO:0000256|HAMAP-Rule:MF_01258}.
SEQUENCE 251 AA; 27498 MW; E512921F6B4F343D CRC64;
MELFPVPDVP EIREGDDLAA LISERVDLRP GDVVCVASTV VSKAEGRFAD LDDFPAGPRA
RELAARLSEL TDDEKDPRFA QAVLEESVDL VMDEPFLLTE TRFGHVGVNA GIDRSNVPDH
DLLLLPKRPN KSAERICAGI TADRVIVSDT CGRPFRHGQR GVALGWAGLS ASRDWRGETD
RDGRELGVTV ESVVDELAAA ANLVQGEGDD GTPVVVVRNF EWGDHGESEA HFRDIDGDFV
RQALRDWSYE P


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