ID   MNMG_CAUVN              Reviewed;         618 AA.
AC   B8GW33; Q9XBF8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=CCNA_03871;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ho H.-Y.H., Draper G.C., Gober J.W.;
RT   "Partial 50K and complete gidA, gidB, parA and parB genes from Caulbacter
RT   crescentus.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
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DR   EMBL; U87804; AAD40695.1; -; Genomic_DNA.
DR   EMBL; CP001340; ACL97336.2; -; Genomic_DNA.
DR   RefSeq; WP_024266007.1; NC_011916.1.
DR   RefSeq; YP_002519244.2; NC_011916.1.
DR   AlphaFoldDB; B8GW33; -.
DR   SMR; B8GW33; -.
DR   PRIDE; B8GW33; -.
DR   EnsemblBacteria; ACL97336; ACL97336; CCNA_03871.
DR   GeneID; 7332719; -.
DR   KEGG; ccs:CCNA_03871; -.
DR   PATRIC; fig|565050.3.peg.3776; -.
DR   HOGENOM; CLU_007831_2_2_5; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   PhylomeDB; B8GW33; -.
DR   Proteomes; UP000001364; 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..618
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000378291"
FT   BINDING         11..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   618 AA;  67169 MW;  D04457A39BFAE36D CRC64;
     MSKSWDVIVI GGGHAGCEAA AASARAGART LLLTHKLETI GEMSCNPAIG GLGKGHLVRE
     IDALDGVMGR MADKAGIQFR MLNRSKGPAV RGPRSQIDRR LYREAMQAEL FSTGNLDIIA
     AAAEDLIVED GKVAGAVDAA GQAYRAPRVI LTTGTFLKGV IHRGEDRIPA GRVGDQPAIG
     LSDRLYGLGF QMGRLKTGTP ARLDGKTIAW DRLESQAADD TPVPFSYLNH RIDVPQIACG
     VTYTTEETHR IIAERIGESL VYSGRATGVG PRYCPSIEDK VVRFADKTSH QIFLEPEGLD
     DDTVYPNGIS TSVSEETQLL FLRTIPGLEQ VEVIRYGYAI EYDYVDPREL YPTLETKRLP
     GLYLAGQING TTGYEEAGAQ GLVAGLNAAL AVQGREPAIF ARDEAYIGVM IDDLVTRGVT
     EPYRMFTSRA EFRLTLRADN ADQRLSDRGI SLGVVGPVRA AAWTEKKARL DAARAFARSV
     TLTPNEAVKA GFKVNSDGVR RDVFAMLAYP DVTLDDLGRI WPEVFTWNTD VREQIEIEAA
     YAGYLDRQRA DAESLRKDED LRLPADLDYA EIGSLSNEVR GKLARVRPLT LGQAARIEGV
     TPGALTALLA HVRRGRAA