ID   COFF_METMP              Reviewed;         285 AA.
AC   Q6M0U8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Coenzyme gamma-F420-2:alpha-L-glutamate ligase;
DE            EC=6.3.2.32;
GN   Name=cofF; OrderedLocusNames=MMP0170;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: Catalyzes the ATP-dependent addition of one alpha-linked L-
CC       glutamate molecule to coenzyme gamma-F420-2, producing coenzyme alpha-
CC       F420-3. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a
CC       terminal alpha-linked glutamate (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + oxidized coenzyme F420-2 = ADP + H(+) +
CC         oxidized coenzyme alpha-F420-3 + phosphate; Xref=Rhea:RHEA:42332,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57922, ChEBI:CHEBI:59923,
CC         ChEBI:CHEBI:456216; EC=6.3.2.32;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RimK family. CofF subfamily. {ECO:0000305}.
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DR   EMBL; BX950229; CAF29726.1; -; Genomic_DNA.
DR   RefSeq; WP_011170114.1; NC_005791.1.
DR   AlphaFoldDB; Q6M0U8; -.
DR   SMR; Q6M0U8; -.
DR   STRING; 267377.MMP0170; -.
DR   EnsemblBacteria; CAF29726; CAF29726; MMP0170.
DR   GeneID; 2761868; -.
DR   KEGG; mmp:MMP0170; -.
DR   PATRIC; fig|267377.15.peg.174; -.
DR   eggNOG; arCOG01589; Archaea.
DR   HOGENOM; CLU_975255_0_0_2; -.
DR   OMA; YEHKVFY; -.
DR   OrthoDB; 42812at2157; -.
DR   BioCyc; MMAR267377:MMP_RS00955-MON; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043774; F:coenzyme F420-2 alpha-glutamyl ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR031039; F420_CofF.
DR   InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 1.
DR   TIGRFAMs; TIGR04443; F420_CofF; 1.
DR   TIGRFAMs; TIGR00768; rimK_fam; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..285
FT                   /note="Coenzyme gamma-F420-2:alpha-L-glutamate ligase"
FT                   /id="PRO_0000205499"
FT   DOMAIN          98..284
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         170..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   285 AA;  32127 MW;  6F16395E96B83A61 CRC64;
     MITIACAEGG STIYSLKKAI EDLGEKCNIL LLSSDNLLVD TDFNIKTDLI HSRCGIGDYL
     DRLTLFSWQV LKNLESEGHY FINPLETIYN SSDKFKTTKI LSKNGLKTPK TALIRDYADA
     KHFLDTKNMN YPVILKNSFS KCGMKVQKAN SDDELKKLSK NSIWESKLIQ EYVDFKNGDT
     YKDMRILVID GEVVGGYRRV SNNFITNLYV GGQIEPLNVS SELEEIALKC SECMNGYIMG
     IDILPKDGEY YVVEVNTAPG TKGFRSLGID VDKRIAECLI KYKKS