MNMG_RICPU
ID MNMG_RICPU Reviewed; 622 AA.
AC C4K176;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129};
GN Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129};
GN Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129};
GN OrderedLocusNames=RPR_02505;
OS Rickettsia peacockii (strain Rustic).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=562019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rustic;
RX PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT with virulent Rickettsia rickettsii: identification of virulence factors.";
RL PLoS ONE 4:E8361-E8361(2009).
CC -!- FUNCTION: NAD-binding protein involved in the addition of a
CC carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of
CC certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-
CC Rule:MF_00129}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC Rule:MF_00129}.
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DR EMBL; CP001227; ACR47327.1; -; Genomic_DNA.
DR AlphaFoldDB; C4K176; -.
DR SMR; C4K176; -.
DR EnsemblBacteria; ACR47327; ACR47327; RPR_02505.
DR KEGG; rpk:RPR_02505; -.
DR HOGENOM; CLU_007831_2_2_5; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000005015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 1.10.150.570; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR044920; MnmG_C_subdom.
DR InterPro; IPR040131; MnmG_N.
DR PANTHER; PTHR11806; PTHR11806; 1.
DR PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00136; gidA; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT CHAIN 1..622
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000203167"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 177
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 622 AA; 68788 MW; 749AD4CBE4262B77 CRC64;
MLKYDVIVIG GGHAGVEAAA ASARLGVPTL LITLKPENLG EMSCNPAIGG IAKGTLVKEI
DALDGLMGYV IDQAGIHYKM LNETRGPAVW GPRAQADRKL YKKAMYQILT NYPNLDILYG
KVEDIEIKSS KIEAVILNNG SKILCQKIIL TTGTFLSGLI HIGQKKIPAG RVDEEPSYGL
SNTLKQIGFK LARLKTGTPP RIDGRTIDYS KTILQPGDKI PRPFSELTNI VNVSQINCFI
TTTTSETHDI IRENLDKSAM YSGQIEGIGP RYCPSIEDKI VRFSTKSEHR IFLEPEGLDD
YTIYPNGIST SLPEDVQHKL IKTIPGLENV KVLRPGYAIE YDYVDPREIS VTLETKKIAG
LYLAGQINGT TGYEEAAGQG IIAGINAALA VKDQAPFMLT RANSYIGVMI DDLTTFGTIE
PYRMFTSRSE YRLSLRADNS DLRLTELGMN IGVVSEKRKK IFTKKCEDIE KIKSLLNTLS
LTTSKLAKMG IQVAQDGTYK TVLDLFKIPN FNVEQAIKIF PMLKETQNNN ILQLLYIEAK
YASYLTRQHA DINLFQSEEA QFIPKNLDYF KIPSISLEIQ EKLSSHKPTT IGVARRIPGI
TPAAITAIII YLKTKYSDGS ST