ID   MPTN_METJA              Reviewed;         291 AA.
AC   Q58037;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Tetrahydromethanopterin:alpha-L-glutamate ligase;
DE            EC=6.3.2.33;
DE   AltName: Full=H(4)MPT:alpha-L-glutamate ligase;
GN   Name=mptN; OrderedLocusNames=MJ0620;
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, 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 or GTP-dependent addition of one L-
CC       glutamate molecule to tetrahydromethanopterin, producing
CC       tetrahydrosarcinapterin. {ECO:0000269|PubMed:12909715}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6,7,8-tetrahydromethanopterin + ATP + L-glutamate = 5,6,7,8-
CC         tetrahydrosarcinapterin + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:30567, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58103,
CC         ChEBI:CHEBI:59924, ChEBI:CHEBI:456216; EC=6.3.2.33;
CC         Evidence={ECO:0000269|PubMed:12909715};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydrosarcinapterin
CC       biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12909715}.
CC   -!- SIMILARITY: Belongs to the RimK family. MptN subfamily. {ECO:0000305}.
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DR   EMBL; L77117; AAB98615.1; -; Genomic_DNA.
DR   PIR; D64377; D64377.
DR   RefSeq; WP_010870125.1; NC_000909.1.
DR   AlphaFoldDB; Q58037; -.
DR   SMR; Q58037; -.
DR   STRING; 243232.MJ_0620; -.
DR   EnsemblBacteria; AAB98615; AAB98615; MJ_0620.
DR   GeneID; 1451486; -.
DR   KEGG; mja:MJ_0620; -.
DR   eggNOG; arCOG01589; Archaea.
DR   HOGENOM; CLU_054353_2_0_2; -.
DR   InParanoid; Q58037; -.
DR   OMA; CYMNIAS; -.
DR   OrthoDB; 42812at2157; -.
DR   PhylomeDB; Q58037; -.
DR   BioCyc; MetaCyc:MON-15293; -.
DR   BRENDA; 6.3.2.33; 3260.
DR   UniPathway; UPA00069; -.
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:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR   Pfam; PF08443; RimK; 1.
DR   TIGRFAMs; TIGR00768; rimK_fam; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..291
FT                   /note="Tetrahydromethanopterin:alpha-L-glutamate ligase"
FT                   /id="PRO_0000205502"
FT   DOMAIN          101..286
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         175..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         261
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ   SEQUENCE   291 AA;  33277 MW;  2B6A3438290A3B0E CRC64;
     MKLGIITIER DAVVNDLIKS CEKYEVDYKV ITPSNIVAGF NLDFKLKYYK SFLDELDCCF
     VRNLGWDSFF RFDVLKYLNH YIPVINPPDG IDRASNKFLT SVFLELNNLP QPKTVVTESI
     NEAIVWIDKF EEAVLKPIFG CGGEGIVRVK KELPISTKLK ILNEFKEKYN TFYIQEFIKP
     VRNEHRDIRA FVVDDEVVAA MYRIGGENWK NNVSQGGRVE KCEITEEIEK LALKAKNALG
     LFYAGVDLIE SEDGLKVLEV NSTPSWIGLS KVSEVNIADK LLEKIIQYVK S