ID   COFF_METJA              Reviewed;         288 AA.
AC   Q58407;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Coenzyme gamma-F420-2:alpha-L-glutamate ligase;
DE            EC=6.3.2.32;
GN   Name=cofF; OrderedLocusNames=MJ1001;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=12909715; DOI=10.1073/pnas.1733391100;
RA   Li H., Xu H., Graham D.E., White R.H.;
RT   "Glutathione synthetase homologs encode alpha-L-glutamate ligases for
RT   methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9785-9790(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent addition of one alpha-linked L-
CC       glutamate molecule to coenzyme gamma-F420-2, producing alpha-F420-3,
CC       the major form of coenzyme F420 found in M.jannaschii. Thus, caps the
CC       gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked
CC       glutamate. Prefers ATP to other purine nucleotide triphosphates; GTP
CC       gives about 25% of the activity observed with ATP. Cannot catalyze the
CC       addition of the following amino acids or analogs: D-glutamate, beta-
CC       glutamate, L-aspartate, L-glutamine, L-alpha-aminoadipate, or D,L-2-
CC       amino-4-phosphono-butyrate. {ECO:0000269|PubMed:12909715}.
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         Evidence={ECO:0000269|PubMed:12909715};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:12909715};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:12909715};
CC   -!- ACTIVITY REGULATION: Inhibited by KCl. {ECO:0000269|PubMed:12909715}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.2 uM for coenzyme F420-2 {ECO:0000269|PubMed:12909715};
CC         Vmax=0.72 nmol/min/mg enzyme {ECO:0000269|PubMed:12909715};
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:12909715};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12909715}.
CC   -!- SIMILARITY: Belongs to the RimK family. CofF subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99004.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99004.1; ALT_INIT; Genomic_DNA.
DR   PIR; H64424; H64424.
DR   RefSeq; WP_064496695.1; NC_000909.1.
DR   AlphaFoldDB; Q58407; -.
DR   SMR; Q58407; -.
DR   STRING; 243232.MJ_1001; -.
DR   EnsemblBacteria; AAB99004; AAB99004; MJ_1001.
DR   GeneID; 1451898; -.
DR   KEGG; mja:MJ_1001; -.
DR   eggNOG; arCOG01589; Archaea.
DR   HOGENOM; CLU_975255_0_0_2; -.
DR   InParanoid; Q58407; -.
DR   OMA; YEHKVFY; -.
DR   OrthoDB; 42812at2157; -.
DR   PhylomeDB; Q58407; -.
DR   BioCyc; MetaCyc:MON-12190; -.
DR   BRENDA; 6.3.2.32; 3260.
DR   SABIO-RK; Q58407; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043774; F:coenzyme F420-2 alpha-glutamyl ligase activity; IDA:MENGO.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Ligase; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..288
FT                   /note="Coenzyme gamma-F420-2:alpha-L-glutamate ligase"
FT                   /id="PRO_0000205498"
FT   DOMAIN          101..287
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         173..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  33112 MW;  08443376FDC5E61D CRC64;
     MVKITILSPE GRSCSVWSLK NEIEKLGAKC DIFLLSSPEN LMSHDFKLET DLIHSRCGIG
     DYFDRLTLYS WQFINALEVE GCRFINPIKT LYLTSDKFKC IKLLAKNKIK TPKTALIRDY
     EDAVKFIEKY NLRFPVVIKN SFSKCGLKVF MARNYDELKQ LTKNAIWEGK LIQEFIDFKE
     NDLYRDMRIL VVDGEVVGGY RRVSRDFRTN LYLGNVVEKL NIDEELEELA LKCADLSEAV
     ILGVDILPTK DNYYVIELNS SPGTKGFRDI GINADKKIAE ALVRYAKS