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Database: UniProt
Entry: A0A154WH81_9PROT
LinkDB: A0A154WH81_9PROT
Original site: A0A154WH81_9PROT 
ID   A0A154WH81_9PROT        Unreviewed;       440 AA.
AC   A0A154WH81;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=AUP43_00385 {ECO:0000313|EMBL:KZD12835.1};
OS   Oceanibaculum pacificum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Oceanibaculaceae; Oceanibaculum.
OX   NCBI_TaxID=580166 {ECO:0000313|EMBL:KZD12835.1, ECO:0000313|Proteomes:UP000076400};
RN   [1] {ECO:0000313|EMBL:KZD12835.1, ECO:0000313|Proteomes:UP000076400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A02656 {ECO:0000313|EMBL:KZD12835.1,
RC   ECO:0000313|Proteomes:UP000076400};
RA   Lu L., Lai Q., Shao Z., Qian P.;
RT   "Genome sequence of Oceanibaculum pacificum MCCC 1A02656.";
RL   Submitted (DEC-2015) 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, 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZD12835.1}.
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DR   EMBL; LPXN01000001; KZD12835.1; -; Genomic_DNA.
DR   RefSeq; WP_067551029.1; NZ_LPXN01000001.1.
DR   AlphaFoldDB; A0A154WH81; -.
DR   STRING; 580166.AUP43_00385; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000076400; 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; TIGR00450; mnmE_trmE_thdF; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF116878; TrmE connector domain; 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   Reference proteome {ECO:0000313|Proteomes:UP000076400};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00379}.
FT   DOMAIN          217..366
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         81
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         121
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         227..232
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         227
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         231
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         246..252
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
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         248
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         251
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         271..274
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00379"
FT   BINDING         440
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   440 AA;  47492 MW;  1B70C31B73444652 CRC64;
     MSGHTIFALA SGAGRSGIAV IRISGPLARQ ALSALTRREL PPPRQASLRL LAMPESGEML
     DHALTLWFPA PHSFTGEDVV ELHLHGGRAV IAGVIEALSA LPDLRLAEPG EFTRRAFLAG
     KLDLTEVEGL ADLIDAETTA QRRQALRQMD GALSGLYEDW RTRLIRCLAH TEAAIDFADE
     ELPADMMLAI QAEVQGLRQE MQAHLADGRR GEMLREGFRI AIIGPPNAGK SSLLNWLAQR
     DAAIVSEIAG TTRDVIEAHL DLGGYSVLLA DTAGLRETVD GIEAEGIRRA RNWAAAADLQ
     LLVLDATQPE PVGTVSDAPM IRVLNKVDLK IKGHTCQSFP IDAMSISVRT GEGLDALLQK
     LTGLVAEKLD MAGTPSLTRE RHRAAVTLCV EALDRFLKGR AADLAAEDMR VALRALGRIT
     GQADVEDLLD VIFRDFCLGK
//
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