ID A0A1I5RDS9_9SPHN Unreviewed; 438 AA.
AC A0A1I5RDS9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 Synonyms=trmE {ECO:0000256|HAMAP-Rule:MF_00379};
GN ORFNames=SAMN04488241_103187 {ECO:0000313|EMBL:SFP56615.1};
OS Sphingomonas rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP56615.1, ECO:0000313|Proteomes:UP000199586};
RN [1] {ECO:0000313|EMBL:SFP56615.1, ECO:0000313|Proteomes:UP000199586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP56615.1,
RC ECO:0000313|Proteomes:UP000199586};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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: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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00379}.
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DR EMBL; FOXP01000003; SFP56615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5RDS9; -.
DR STRING; 634430.SAMN04488241_103187; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000199586; Unassembled WGS sequence.
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 NCBIfam; TIGR00231; small_GTP; 1.
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; SSF103025; Folate-binding domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Reference proteome {ECO:0000313|Proteomes:UP000199586};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00379}.
FT DOMAIN 17..131
FT /note="GTP-binding protein TrmE N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10396"
FT DOMAIN 134..435
FT /note="MnmE helical"
FT /evidence="ECO:0000259|Pfam:PF12631"
FT DOMAIN 231..318
FT /note="G"
FT /evidence="ECO:0000259|Pfam:PF01926"
FT BINDING 34
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 91
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 131
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 239..244
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 239
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 258..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 258
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 260
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 263
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 283..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT BINDING 438
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 438 AA; 45801 MW; 0BF7BF69E2772D9F CRC64;
MATAAGRHDE ARGVTDTIVA LSSGRPPAAI GVIRVSGPAA LVAAATLAGT LPPPRIAGLR
ALRDANGAML DRALVLVFPG SRSATGEDLV EFHCHGGRAV IAAVEAALVA ATGCRAALPG
EFTRRALTNG RIDLAEAEGL ADLLEAETEA QRVAALAAAE GRISRQVATW MASAAAISAR
IEALIDHDDE GDVETGEEVL AAIMADAAVL GTEIAFAVEA PPVERLRDGV RVVIAGPPNA
GKSTLLNLLG EREAAIVSPI AGTTRDMVEA PVVRRGRAFV LTDTAGLTRS DDVVEMIGVD
RARYAIEAAD ILLWLGDEPP PRDDAIPIHS RADAAERRVV PAGRLAISRD APRSIESLWN
VIEERASALL PRIDGLPWRQ RHQQLCGEAA AALLQGSNDP VLLAENCRTA RVRLAAIVGI
DATEAMLDAL FSRFCLGK
//