MNME_THEMA
ID MNME_THEMA Reviewed; 450 AA.
AC Q9WYA4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379};
DE EC=3.6.5.-;
GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN Synonyms=trmE {ECO:0000255|HAMAP-Rule:MF_00379}; OrderedLocusNames=TM_0267;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP CHARACTERIZATION.
RX PubMed=11092873; DOI=10.1128/jb.182.24.7078-7082.2000;
RA Yamanaka K., Hwang J., Inouye M.;
RT "Characterization of GTPase activity of TrmE, a member of a novel GTPase
RT superfamily, from Thermotoga maritima.";
RL J. Bacteriol. 182:7078-7082(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH
RP FORMYLTETRAHYDROFOLATE, GTP-BINDING, AND SUBUNIT.
RX PubMed=15616586; DOI=10.1038/sj.emboj.7600507;
RA Scrima A., Vetter I.R., Armengod M.-E., Wittinghofer A.;
RT "The structure of the TrmE GTP-binding protein and its implications for
RT tRNA modification.";
RL EMBO J. 24:23-33(2005).
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.
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; AE000512; AAD35356.1; -; Genomic_DNA.
DR PIR; A72397; A72397.
DR RefSeq; NP_228080.1; NC_000853.1.
DR RefSeq; WP_004082971.1; NZ_CP011107.1.
DR PDB; 1XZP; X-ray; 2.30 A; A=1-450, B=1-118.
DR PDB; 1XZQ; X-ray; 2.90 A; A=1-450, B=1-117.
DR PDBsum; 1XZP; -.
DR PDBsum; 1XZQ; -.
DR AlphaFoldDB; Q9WYA4; -.
DR SMR; Q9WYA4; -.
DR STRING; 243274.THEMA_03390; -.
DR EnsemblBacteria; AAD35356; AAD35356; TM_0267.
DR KEGG; tma:TM0267; -.
DR eggNOG; COG0486; Bacteria.
DR InParanoid; Q9WYA4; -.
DR OMA; CEIQCHG; -.
DR OrthoDB; 263682at2; -.
DR EvolutionaryTrace; Q9WYA4; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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; IPR008144; Guanylate_kin-like_dom.
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 PRINTS; PR00326; GTP1OBG.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; tRNA processing.
FT CHAIN 1..450
FT /note="tRNA modification GTPase MnmE"
FT /id="PRO_0000188939"
FT DOMAIN 211..372
FT /note="TrmE-type G"
FT BINDING 20
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 ECO:0000269|PubMed:15616586"
FT BINDING 78
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 ECO:0000269|PubMed:15616586"
FT BINDING 117
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 ECO:0000269|PubMed:15616586"
FT BINDING 221..226
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 221
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 240..246
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 240
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 242
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 245
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 265..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 326..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 353..355
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 450
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 ECO:0000269|PubMed:15616586"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1XZP"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 148..172
FT /evidence="ECO:0007829|PDB:1XZP"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 181..210
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 307..316
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 360..370
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 386..407
FT /evidence="ECO:0007829|PDB:1XZP"
FT HELIX 412..429
FT /evidence="ECO:0007829|PDB:1XZP"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1XZQ"
FT HELIX 436..443
FT /evidence="ECO:0007829|PDB:1XZP"
SQ SEQUENCE 450 AA; 50682 MW; 8DAD2D1EB8500CC0 CRC64;
MDTIVAVATP PGKGAIAILR LSGPDSWKIV QKHLRTRSKI VPRKAIHGWI HENGEDVDEV
VVVFYKSPKS YTGEDMVEVM CHGGPLVVKK LLDLFLKSGA RMAEPGEFTK RAFLNGKMDL
TSAEAVRDLI EAKSETSLKL SLRNLKGGLR DFVDSLRREL IEVLAEIRVE LDYPDEIETN
TGEVVTRLER IKEKLTEELK KADAGILLNR GLRMVIVGKP NVGKSTLLNR LLNEDRAIVT
DIPGTTRDVI SEEIVIRGIL FRIVDTAGVR SETNDLVERL GIERTLQEIE KADIVLFVLD
ASSPLDEEDR KILERIKNKR YLVVINKVDV VEKINEEEIK NKLGTDRHMV KISALKGEGL
EKLEESIYRE TQEIFERGSD SLITNLRQKQ LLENVKGHLE DAIKSLKEGM PVDMASIDLE
RALNLLDEVT GRSFREDLLD TIFSNFCVGK
