COFE_HALLT
ID COFE_HALLT Reviewed; 251 AA.
AC B9LPH6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01258};
DE EC=6.3.2.31 {ECO:0000255|HAMAP-Rule:MF_01258};
DE EC=6.3.2.34 {ECO:0000255|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01258};
GN Name=cofE {ECO:0000255|HAMAP-Rule:MF_01258}; OrderedLocusNames=Hlac_1679;
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01258};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01258};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01258};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000255|HAMAP-Rule:MF_01258};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01258};
CC Note=Monovalent cation. The ion could be potassium. {ECO:0000255|HAMAP-
CC Rule:MF_01258};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01258}.
CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000255|HAMAP-
CC Rule:MF_01258}.
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DR EMBL; CP001365; ACM57264.1; -; Genomic_DNA.
DR RefSeq; WP_015910402.1; NC_012029.1.
DR AlphaFoldDB; B9LPH6; -.
DR SMR; B9LPH6; -.
DR STRING; 416348.Hlac_1679; -.
DR EnsemblBacteria; ACM57264; ACM57264; Hlac_1679.
DR GeneID; 7400436; -.
DR KEGG; hla:Hlac_1679; -.
DR eggNOG; arCOG02714; Archaea.
DR HOGENOM; CLU_051152_1_1_2; -.
DR OMA; KHGFVCA; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000740; Chromosome 1.
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 3: Inferred from homology;
KW GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Potassium.
FT CHAIN 1..251
FT /note="Coenzyme F420:L-glutamate ligase"
FT /id="PRO_1000165111"
FT BINDING 9..12
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 38..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 113
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 150
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 205..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 207
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
SQ SEQUENCE 251 AA; 27294 MW; C79F8CB83B1A221F CRC64;
MELFAVPGLP EIRDGDDLAA MIDERVDLRE GDVVVVASTV VSKAEGRTFD LSDFPASERA
EAVADRLAEI AGEEKDPRFA QAVIEESTEL IMEAPFLLTA TRFGHIGVNA GIDQSNVPDG
DLLLLPERPS ESAARIREGI AADRVVVSDT CGRPFRHGQR GVAIGWAGLP ASRDWRGERD
RDGREMGVTV QNVIDELASA ANLVAGEGDG GTPVVVVRDW EFGDHDGSDN HFREVEGDFV
RQALRQWTFD D
