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MNME_GEOTN
ID   MNME_GEOTN              Reviewed;         462 AA.
AC   A4ITX1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379};
DE            EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379};
GN   Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN   Synonyms=trmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN   OrderedLocusNames=GTNG_3440;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate.
CC       Involved in the addition of a carboxymethylaminomethyl (cmnm) group at
CC       the wobble position (U34) of certain tRNAs, forming tRNA-
CC       cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00379}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00379};
CC       Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00379};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00379}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00379}.
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DR   EMBL; CP000557; ABO68775.1; -; Genomic_DNA.
DR   RefSeq; WP_008880828.1; NC_009328.1.
DR   AlphaFoldDB; A4ITX1; -.
DR   SMR; A4ITX1; -.
DR   STRING; 420246.GTNG_3440; -.
DR   EnsemblBacteria; ABO68775; ABO68775; GTNG_3440.
DR   KEGG; gtn:GTNG_3440; -.
DR   eggNOG; COG0486; Bacteria.
DR   HOGENOM; CLU_019624_4_1_9; -.
DR   OMA; CEIQCHG; -.
DR   OrthoDB; 263682at2; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd04164; trmE; 1.
DR   Gene3D; 1.20.120.430; -; 1.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00379; GTPase_MnmE; 1.
DR   InterPro; IPR031168; G_TrmE.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR018948; GTP-bd_TrmE_N.
DR   InterPro; IPR004520; GTPase_MnmE.
DR   InterPro; IPR027368; MnmE_dom2.
DR   InterPro; IPR025867; MnmE_helical.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF12631; MnmE_helical; 1.
DR   Pfam; PF10396; TrmE_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51709; G_TRME; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Potassium; tRNA processing.
FT   CHAIN           1..462
FT                   /note="tRNA modification GTPase MnmE"
FT                   /id="PRO_1000048829"
FT   DOMAIN          224..383
FT                   /note="TrmE-type G"
FT   BINDING         23
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         88
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         127
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         234..239
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         234
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         253..259
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         253
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         255
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         258
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         278..281
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         462
FT                   /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57457"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
SQ   SEQUENCE   462 AA;  51264 MW;  2C9E4BCC42A1E3A6 CRC64;
     MTEFDTIAAI STPMGEGAIA IVRLSGDEAV EIADRLFRSP TGKQLKDVPS HTIHYGHIVD
     PKSGRIVEEV MVSVMRAPKT FTREDVVEIN CHGGFVSVNR VLQLVLANGA RLAEPGEFTK
     RAFLNGRIDL SQAEAVIDLI RAKTDRAMNV ALQQMEGRLS KLIRELRQTI LETLAHVEVN
     IDYPEYDDVE EMTPRLLKEK AEYVRGQIEK LLSTATQGKI LREGLATVII GRPNVGKSSL
     LNALAHENRA IVTDIPGTTR DVIEEYVNVR GVPLRLIDTA GIRETEDIVE RIGVERSRQM
     LKKADLILLV LNYHEPLTEE DERLFAMTEG MDVIVIVNKT DLPQNIDIER VKELAAGRPI
     VATSLLCERG IDELEKAIAD LFFGGELEAG DLTYVSNSRH IALLEQAKKA IEDALSGIDV
     GMPVDLVQID LRRAWELLGE IVGDTVHESL IDQLFAQFCL GK
 
 
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