ID   MNMG_BRUAB              Reviewed;         636 AA.
AC   Q57AJ7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=BruAb1_2036;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(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; AE017223; AAX75337.1; -; Genomic_DNA.
DR   RefSeq; WP_002967028.1; NC_006932.1.
DR   AlphaFoldDB; Q57AJ7; -.
DR   SMR; Q57AJ7; -.
DR   EnsemblBacteria; AAX75337; AAX75337; BruAb1_2036.
DR   GeneID; 3788723; -.
DR   KEGG; bmb:BruAb1_2036; -.
DR   HOGENOM; CLU_007831_2_2_5; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000540; Chromosome I.
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..636
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117069"
FT   BINDING         15..20
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         274..288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   636 AA;  69432 MW;  07B2A517DCF237E0 CRC64;
     MSSAEALAFD VIVIGGGHAG CEAASAAARA GARTALVTHR FDTIGVMSCN PAIGGLGKGH
     LVREIDALDG LMGRVADRAG IQFRLLNRRK GPAVRGPRTQ ADRKLYRLAM QQMITEQENL
     TVVEGGAADL VCDGERISGV TLADGRVLKC GAVVLTTGTF LNGLIHIGEK RFPAGRMGEK
     PALGLSERLL SFGFTLGRLK TGTPPRLDGR TIDWQSLDMQ SADEEPVPFS LMTDRITTPQ
     IECGITRTTP ETHDIIRANL HRSAMYSGSI EGIGPRYCPS VEDKIVKFGD RDGHQIFLEP
     EGLDDDTVYP NGISTSLPED VQLEILKTIP GLEKAVLLQP GYAIEYDFID PRELKRSLET
     RKVCGLFLAG QINGTTGYEE AGAQGLLAGL NAARRAAGSE PVILQRTEAY IGVMVDDLTS
     RGVSEPYRMF TSRAEFRLSL RADNADQRLT PLADEVGILS EERRKRYLTR ETALSHARMV
     TQSLSITPNL AGYYDLRLNQ DGVRRSAYDL LSYPDINLDR LIAIWPELAS IDPVTREALE
     IEAQYAVYME RQQSDIAVME REERLLIPSG LDFDAISGLS NELKQKLKQR KPETIAEAQR
     VDGMTPAAVA LLIAQIRKFG GRQKLAAETL EGKGAA