MPTN_METMA
ID MPTN_METMA Reviewed; 324 AA.
AC Q8Q0M5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=MM_0111;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM29807.1; -; Genomic_DNA.
DR RefSeq; WP_011032065.1; NC_003901.1.
DR AlphaFoldDB; Q8Q0M5; -.
DR SMR; Q8Q0M5; -.
DR STRING; 192952.MM_0111; -.
DR EnsemblBacteria; AAM29807; AAM29807; MM_0111.
DR GeneID; 1478453; -.
DR GeneID; 66134717; -.
DR KEGG; mma:MM_0111; -.
DR PATRIC; fig|192952.21.peg.124; -.
DR eggNOG; arCOG01589; Archaea.
DR HOGENOM; CLU_054353_2_0_2; -.
DR OMA; CYMNIAS; -.
DR UniPathway; UPA00069; -.
DR Proteomes; UP000000595; 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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 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..324
FT /note="Tetrahydromethanopterin:alpha-L-glutamate ligase"
FT /id="PRO_0000205505"
FT DOMAIN 113..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 268..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 195..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 265
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 324 AA; 35037 MW; 1B92FF45C5425AEB CRC64;
MKKIGIAITD PEDWTARALI KAAKEKGFSP LVFDLSDAEV RIGSGISEPA SIFKAGEVLL
SDLDALIVRD VGAGAFEGVS FRFDILRELE AEGVSVINSP EAIQNAANKY HASYLLAKAG
LPVPETVAVQ SLEAALKVIS EFGDAVIKPV FGYKGKDIAR VKNREIRFSD RKIEPAPVEE
ILEKLLEEKG MLYIQEFIEN PGRDIRAFVV GGTAIGAIYR KAAAGSWVNN LSQGGSSDRC
VLTDEQEKIA EKASLALGTT FAGIDIIEGT EESEENKKTE GMSSENRKSP RILEVNGTPS
GKGIFDAWGI NPADHILEYL KNIL
