MNME_CUPPJ
ID MNME_CUPPJ Reviewed; 475 AA.
AC Q46VM0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=Reut_A3456;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ62814.1; -; Genomic_DNA.
DR RefSeq; WP_011299582.1; NC_007347.1.
DR AlphaFoldDB; Q46VM0; -.
DR SMR; Q46VM0; -.
DR STRING; 264198.Reut_A3456; -.
DR EnsemblBacteria; AAZ62814; AAZ62814; Reut_A3456.
DR KEGG; reu:Reut_A3456; -.
DR eggNOG; COG0486; Bacteria.
DR HOGENOM; CLU_019624_4_1_4; -.
DR OMA; CEIQCHG; -.
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 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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; tRNA processing.
FT CHAIN 1..475
FT /note="tRNA modification GTPase MnmE"
FT /id="PRO_0000345880"
FT DOMAIN 220..397
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 124
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 230..235
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 230
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 249..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 249
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 251
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 254
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 274..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 378..380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 475
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 475 AA; 51144 MW; A5362CF64861B870 CRC64;
MTAPLPPIAA IATAPGRGGI GVVRVSGPDV RPVMHAICGQ ALKPRHATYL PFLDGHGKVI
DHGLALYFPG PNSYTGEEVL ELQGHGGPVV MQMLLTRCLQ AGHGIGLRLA EPGEFTRRAF
LNDKLDLAQA EAVADLIEAS TEAAARSAAR SMEGEFSHAI HTLVEKVIHL RMLVEATLDF
PEEEIDFLEA SDARGQLATI RNDLGNVLAQ ARQGALLREG LSVVLAGQPN VGKSSLLNAL
AGAELAIVTP IAGTTRDRVK ETIQIEGIPL HIIDTAGLRD EATDEVERIG IERTWDAIRR
ADIVLHLVDA TDYLRHGLSE IDDAIDDRLS GQLPPGAPIV RVVNKIDVAP TVGGMMFSGN
RPHVVAANGP NPTEIWISAR TGSGIELLRK ELLRLVGWQS GNEGTFLARE RHLTALRQAQ
SHLDVAAEQS ERQAQALDLF AEELRLAQEH LNSITGEFTS DDLLGTIFTR FCIGK
