MNMG_THEYD
ID MNMG_THEYD Reviewed; 624 AA.
AC B5YJL3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=THEYE_A0585;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001147; ACI21694.1; -; Genomic_DNA.
DR RefSeq; WP_012546402.1; NC_011296.1.
DR RefSeq; YP_002248428.1; NC_011296.1.
DR AlphaFoldDB; B5YJL3; -.
DR SMR; B5YJL3; -.
DR STRING; 289376.THEYE_A0585; -.
DR PRIDE; B5YJL3; -.
DR EnsemblBacteria; ACI21694; ACI21694; THEYE_A0585.
DR KEGG; tye:THEYE_A0585; -.
DR PATRIC; fig|289376.4.peg.579; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_0; -.
DR InParanoid; B5YJL3; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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; Reference proteome; tRNA processing.
FT CHAIN 1..624
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000122756"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 272..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 624 AA; 69865 MW; 23340A6A07D5AC36 CRC64;
MYKEKDFDII VVGAGHAGCE AALATAKMGL QTALFTIYLE TIAQLSCNPA IGGLAKGHLV
REIDALGGIM AKVTDMAGIQ FRMLNRSKGP AVWSLRAQAD RILYNIYMRK ILESTENLAI
KQAMVEEIVV ENGKVKGIIT SLGVFYGAKA VIITPGTFLN GLIHIGLDSF EAGRAGEFPS
KKLSESIKKL GLKMGRLKTG TPPRIDAKTI DFSKTEEQGG DDPPIPFSYS TKKINNPQVP
CYITYTNEKT HEIILNNLDR SPLYSGKIKG IGPRYCPSIE DKVVKFRDKS RHQIFLEPEG
LSRKEYYANG IPTSLPYDVQ VAFVRTIPGL EDAEIMRPGY AIEYDFVYPT QIRHTLEVKG
IEGLYLAGQI NGTSGYEEAA AQGLMAGINA ALKIKKQPPL ILGRDEAYIG VLIDDLVTKG
TQEPYRMFTS RAEFRLLLRH DNADLRLRDY GYKIGLVDEE TYEEFNKKKE LLQREIKRLK
TTTIKPSEEL NKALIEAQTT PVEEATFLDK LLKRPELNYD FIKKFAPSEV TLTKELEELV
EIHIKYEGYI AKQMELVERM KQFEEKLIPE NFDFNIPGLS REVIQKLTEV APRTIGQAMR
IPGVTPAAIS ILMVAVQKKT TVKK
