ID A0A3G2QE10_9VIBR Unreviewed; 453 AA. AC A0A3G2QE10; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 03-MAY-2023, entry version 15. DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000256|HAMAP-Rule:MF_00379}; DE EC=3.6.-.- {ECO:0000256|HAMAP-Rule:MF_00379}; GN Name=mnmE {ECO:0000256|HAMAP-Rule:MF_00379, GN ECO:0000313|EMBL:QGH48740.1}; GN Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379}; GN ORFNames=APZ19_17285 {ECO:0000313|EMBL:QGH48740.1}; OS Vibrio owensii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=696485 {ECO:0000313|EMBL:QGH48740.1, ECO:0000313|Proteomes:UP000390336}; RN [1] {ECO:0000313|EMBL:QGH48740.1, ECO:0000313|Proteomes:UP000390336} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SH14 {ECO:0000313|EMBL:QGH48740.1, RC ECO:0000313|Proteomes:UP000390336}; RX PubMed=26634753; RA Liu L., Xiao J., Xia X., Pan Y., Yan S., Wang Y.; RT "Draft Genome Sequence of Vibrio owensii Strain SH-14, Which Causes Shrimp RT Acute Hepatopancreatic Necrosis Disease."; RL Genome Announc. 3:e01395-15(2015). 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:0000256|HAMAP-Rule:MF_00379}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00379}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00379}; CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits. CC {ECO:0000256|HAMAP-Rule:MF_00379}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00379}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. TrmE GTPase family. {ECO:0000256|ARBA:ARBA00011043, CC ECO:0000256|HAMAP-Rule:MF_00379, ECO:0000256|RuleBase:RU003313}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00379}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP045859; QGH48740.1; -; Genomic_DNA. DR RefSeq; WP_005440826.1; NZ_VTXX01000015.1. DR AlphaFoldDB; A0A3G2QE10; -. DR EnsemblBacteria; AYO16115; AYO16115; D0812_17620. DR GeneID; 47099803; -. DR KEGG; vow:A9237_08320; -. DR OrthoDB; 9805918at2; -. DR Proteomes; UP000390336; Chromosome 1. 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 CDD; cd14858; TrmE_N; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.120.430; tRNA modification GTPase MnmE domain 2; 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 PANTHER; PTHR42714; TRNA MODIFICATION GTPASE GTPBP3; 1. DR PANTHER; PTHR42714:SF2; TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF12631; MnmE_helical; 1. DR Pfam; PF10396; TrmE_N; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF116878; TrmE connector domain; 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 {ECO:0000256|HAMAP-Rule:MF_00379}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00379}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00379}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00379}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00379}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00379}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00379}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00379}. FT DOMAIN 215..376 FT /note="TrmE-type G" FT /evidence="ECO:0000259|PROSITE:PS51709" FT BINDING 22 FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57457" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 79 FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57457" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 119 FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57457" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 225..230 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 225 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 229 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 244..250 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 244 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 246 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 249 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 250 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 269..272 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379" FT BINDING 334..337 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00379" SQ SEQUENCE 453 AA; 49214 MW; 9F66C5BD5169F460 CRC64; MTTDTIVAQA TAPGRGGVGI IRVSGPKANQ VALEVTGKTL KPRYAEYLPF QAEDGTVLDQ GIALYFPNPH SFTGEDVLEL QGHGGPVVMD MLIKRILGID GVRAARPGEF SERAFLNDKM DLTQAEAIAD LIDASSEEAA KSALQSLQGQ FSQRIQTLVE SLIHLRIYVE AAIDFPEEEI DFLADGKVSG DLQTIIDNLD AVRKEANQGA IMREGMKVVI AGRPNAGKSS LLNALSGKES AIVTDIAGTT RDVLREHIHI DGMPLHIIDT AGLRDASDEV EKIGIERAWD EIAQADRVLF MVDGTTTDAT DPKDIWPDFV DRLPNSIGMT VIRNKADQTG EDMGICHVND PTLIRLSAKT GAGVDALRTH LKECMGFSGN TEGGFMARRR HLDALERAAQ HLQIGQEQLE GYMAGEILAE ELRITQQHLN EITGEFSSDD LLGRIFSSFC IGK //