ID S6D0G0_9EURY Unreviewed; 251 AA.
AC S6D0G0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Coenzyme F420:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
DE EC=6.3.2.31 {ECO:0000256|HAMAP-Rule:MF_01258};
DE EC=6.3.2.34 {ECO:0000256|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-0:L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01258};
GN Name=cofE {ECO:0000256|HAMAP-Rule:MF_01258,
GN ECO:0000313|EMBL:ERJ07625.1};
GN ORFNames=HLRTI_000378 {ECO:0000313|EMBL:ERJ07625.1}, HTIA_1289
GN {ECO:0000313|EMBL:CCQ33423.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:CCQ33423.1, ECO:0000313|Proteomes:UP000015381};
RN [1] {ECO:0000313|EMBL:ERJ07625.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ07625.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ07625.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ07625.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
RN [3] {ECO:0000313|EMBL:CCQ33423.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC SARL4B {ECO:0000313|EMBL:CCQ33423.1};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(2014).
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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01258};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
CC Note=Monovalent cation. The ion could be potassium. {ECO:0000256|HAMAP-
CC Rule:MF_01258};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01258};
CC Note=Binds 2 divalent metal cations per subunit. The ions could be
CC magnesium and/or manganese. {ECO:0000256|HAMAP-Rule:MF_01258};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01258}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01258}.
CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000256|HAMAP-
CC Rule:MF_01258}.
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DR EMBL; HF571520; CCQ33423.1; -; Genomic_DNA.
DR EMBL; AFNT02000002; ERJ07625.1; -; Genomic_DNA.
DR RefSeq; WP_020936163.1; NZ_AFNT02000002.1.
DR STRING; 1033806.HTIA_1289; -.
DR GeneID; 23800151; -.
DR KEGG; hti:HTIA_1289; -.
DR PATRIC; fig|1033806.12.peg.1282; -.
DR eggNOG; arCOG02714; Archaea.
DR HOGENOM; CLU_051152_1_1_2; -.
DR OrthoDB; 11383at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR Proteomes; UP000015381; Chromosome.
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 Gene3D; 3.30.1330.100; CofE-like; 1.
DR Gene3D; 3.90.1660.10; CofE-like domain; 1.
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 NCBIfam; TIGR01916; F420_cofE; 1.
DR PANTHER; PTHR47917; -; 1.
DR PANTHER; PTHR47917:SF1; COENZYME F420:L-GLUTAMATE LIGASE; 1.
DR Pfam; PF01996; F420_ligase; 1.
DR SUPFAM; SSF144010; CofE-like; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01258};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01258};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01258};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01258};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01258};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01258};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01258}.
FT DOMAIN 9..218
FT /note="Coenzyme F420:L-glutamate ligase-like"
FT /evidence="ECO:0000259|Pfam:PF01996"
FT BINDING 9..12
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 38..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01258"
FT BINDING 116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 149
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 204..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01258"
SQ SEQUENCE 251 AA; 27166 MW; 4EAF6C55EDD5F154 CRC64;
MEVFAVPDIP EIEPGDDLAT LIDERVDLRE GDVLTVASTV VSKAEGRGAD LSDFEAGEHA
RDIADQIGEI AGERKDPRFA QAVIEESEEL VMAAPFILAV TRFGHITVNA GIDRSNVPGA
DLLLLPEDPS ASARRLSDAL GVPVVVTDTS GRPFRQGQRG VAIGWAGLPA MRDWRGEHDR
EGRELTATVE AVVDELAAAT NLVTGEGDDG RPVAVVRDWE FGDHDGHDHL FRDRDGDLVR
QALADFEYHS E
//
