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MNME_RHOP5
ID   MNME_RHOP5              Reviewed;         453 AA.
AC   Q07UP2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 94.
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=RPE_0383;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ04342.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000463; ABJ04342.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041800215.1; NC_008435.1.
DR   AlphaFoldDB; Q07UP2; -.
DR   SMR; Q07UP2; -.
DR   STRING; 316055.RPE_0383; -.
DR   EnsemblBacteria; ABJ04342; ABJ04342; RPE_0383.
DR   KEGG; rpe:RPE_0383; -.
DR   eggNOG; COG0486; Bacteria.
DR   HOGENOM; CLU_019624_3_1_5; -.
DR   OrthoDB; 263682at2; -.
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..453
FT                   /note="tRNA modification GTPase MnmE"
FT                   /id="PRO_0000345891"
FT   DOMAIN          218..379
FT                   /note="TrmE-type G"
FT   BINDING         24
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         81
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         121
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         228..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         247..253
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         253
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         272..275
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT   BINDING         453
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   453 AA;  48271 MW;  CA7067E1144D84A5 CRC64;
     MHASDQTIFA LSSGRPPSAI AIVRVSGSRG AKIVEALAGR LPTPRMAMRA LIKDRDGEPI
     DDAVVLWFPG PASATGEDVA EFHIHGGRAV LAALMATLSS FENVRAAEPG EFTRRAFEHG
     KIDLTEAEGL DDLIHADTDR QRRQALRQLN GLLGDRARDW RAQIIEAQAL IEAGIDFADE
     GDVPDDLLAP ALAKIEALAG EIEALLAAQG RSERLRDGLV VAIVGPPNVG KSTLMNQLAR
     REVAIVSPHA GTTRDVIEVH LDLDGYPVTV IDTAGIRDSD DPVEQEGVRR AQARAAEADL
     VLWLLADDQV AAPAAIESDA PVWLVRNKVD LAGAATGVKP AKNLEANLGQ NVPQPSFAIS
     AKRGDGIADL VGALGGFAAE FFGAGEAGAI TRQRHRDLLR DALVMLQCSK RGRAEELVAE
     DLRSASRSLG RLLGQVDVED VLDALFRDFC IGK
 
 
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