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MNMG_XANOR
ID   MNMG_XANOR              Reviewed;         634 AA.
AC   Q5H6D9;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; OrderedLocusNames=XOO0227;
OS   Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC10331 / KXO85;
RX   PubMed=15673718; DOI=10.1093/nar/gki206;
RA   Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA   Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA   Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA   Go S.-J.;
RT   "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT   bacterial blight pathogen of rice.";
RL   Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW73481.1; -; Genomic_DNA.
DR   RefSeq; WP_011257198.1; NC_006834.1.
DR   AlphaFoldDB; Q5H6D9; -.
DR   SMR; Q5H6D9; -.
DR   STRING; 291331.XOO0227; -.
DR   EnsemblBacteria; AAW73481; AAW73481; XOO0227.
DR   KEGG; xoo:XOO0227; -.
DR   PATRIC; fig|291331.8.peg.259; -.
DR   HOGENOM; CLU_007831_2_2_6; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000006735; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..634
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117220"
FT   BINDING         14..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         279..293
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   634 AA;  68949 MW;  4B4CF5760061153D CRC64;
     MSDSFYRYDV IVIGGGHAGT EAALASARAG AHTLLLTHTI ETVGAMSCNP AIGGIGKGHL
     VKEIDALGGA MAHAADLAGI QWRTLNASKG PAVRATRCQA DRNLYRTAIR CIVQAQPKLT
     VFQAAVDDLI IHNGTCEADS VRGVITQTGL RFEAPSVVLT AGTFLAGKIH VGDTQYAAGR
     LGDPPATTLA ARLRERPFAI DRLKTGTPPR IDGRTLDYGV MGEQPGDDPL PVMSFMGQVS
     DHPRQVSCWI TQTTEQTHDI IRNALHRSPL YSGQIEGIGP RYCPSIEDKV VRFAEKTSHQ
     IFVEPEGLDV AEIYPNGIST SLPFDVQLAL VRSIHGFAQA HITRPGYAIE YDFFDPRGLK
     ASLETKAVGG LFFAGQINGT TGYEEAAAQG LLAGLNAARH VHGLPAWSPR RDEAYLGVLV
     DDLITHGTTE PYRMFTSRAE YRLQLREDNA DARLTGAGRE MGLVDDARWA RFSAKQEAVQ
     RETARLSALW ATPGNALGRE VADALGVTVS RETNVLDLIK RPELNYATLM RVPTLGPGVD
     DAQVAEQVEI SVKYTGYLDR QRDDIARQQR HETTPIPEGF DYAGVRGLSI EVQQKLEHVR
     PQHIGQAQRI PGMTPAAISL LLVHLERARR HRVA
 
 
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