MPTN_METMP
ID MPTN_METMP Reviewed; 292 AA.
AC Q6LZC7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=MMP0702;
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 or GTP-dependent addition of one L-
CC glutamate molecule to tetrahydromethanopterin, producing
CC tetrahydrosarcinapterin. {ECO:0000250}.
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 -!- 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:0000250}.
CC -!- SIMILARITY: Belongs to the RimK family. MptN subfamily. {ECO:0000305}.
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DR EMBL; BX950229; CAF30258.1; -; Genomic_DNA.
DR RefSeq; WP_011170646.1; NC_005791.1.
DR AlphaFoldDB; Q6LZC7; -.
DR SMR; Q6LZC7; -.
DR STRING; 267377.MMP0702; -.
DR EnsemblBacteria; CAF30258; CAF30258; MMP0702.
DR GeneID; 2762372; -.
DR KEGG; mmp:MMP0702; -.
DR PATRIC; fig|267377.15.peg.719; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_0_2; -.
DR OMA; CYMNIAS; -.
DR OrthoDB; 42812at2157; -.
DR BioCyc; MMAR267377:MMP_RS03675-MON; -.
DR UniPathway; UPA00069; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding; GTP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..292
FT /note="Tetrahydromethanopterin:alpha-L-glutamate ligase"
FT /id="PRO_0000205503"
FT DOMAIN 103..286
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 176..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 204
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 292 AA; 33016 MW; 7658A4E682AF8784 CRC64;
MRMGIISEER DWVTDELKSK MEKNDIDPVI IQPSKIISYI ESEVKFEQNN RSILDLKCAF
VRNIGEGVEM FHRFDMLKYL ENYVPIINPM DGIENAGNKF RTSFLMEVHK IPHPKTIVAE
DVNKALIAAD KFEDVVLKPL FGNQGKGLVR VKGRSTVAKL KALNTFKSTH GVIYMQEFVN
NPNNVYRDIR AFVVGDKVIS AMYRTSDNWI TNIHQNGVPE KCEITEELSK IVLAAKDAVG
LVYAGVDILE SSDGLKVIEV NACPSWEGLS RISEVDIAQN LIDEALNYAK EY
