COFE_HALMA
ID COFE_HALMA Reviewed; 257 AA.
AC Q5UZQ7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=rrnAC2436;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47246.1; -; Genomic_DNA.
DR RefSeq; WP_007189416.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UZQ7; -.
DR SMR; Q5UZQ7; -.
DR STRING; 272569.rrnAC2436; -.
DR EnsemblBacteria; AAV47246; AAV47246; rrnAC2436.
DR GeneID; 40153336; -.
DR KEGG; hma:rrnAC2436; -.
DR PATRIC; fig|272569.17.peg.3049; -.
DR eggNOG; arCOG02714; Archaea.
DR HOGENOM; CLU_051152_1_1_2; -.
DR OMA; KHGFVCA; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000001169; Chromosome I.
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; Reference proteome.
FT CHAIN 1..257
FT /note="Coenzyme F420:L-glutamate ligase"
FT /id="PRO_0000145786"
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 154
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 155
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 210..217
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01258"
FT BINDING 212
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 257 AA; 27600 MW; 19ABF7A45C694C0F CRC64;
MEVFAVEGVP EVRPGDDVAE LLVEQADLQD DDVVCVASTI VSKANGRGRS LSSYEPSGRA
ERIAATIEDI ADEEKDPRMA QAILDECEEV LVEAPFILGV TKFGHITVNA GIDRSNVPGA
DLLLLPEDPT AEAEAIRDGI REHAGVEPSV IVTDTSGRPF RLGQRGVALG WAGLSASRDW
RGEHDRDGRE LEATVQAVVD ELAAAANLVT GEGDGGTPAA VVRDFDFGDH AGSEQLFRDP
EKDVVRQALR EWSHVRD
