ID   MNMG_CAMHC              Reviewed;         640 AA.
AC   A7I199;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=CHAB381_0710;
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) 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; CP000776; ABS51738.1; -; Genomic_DNA.
DR   RefSeq; WP_012108577.1; NC_009714.1.
DR   AlphaFoldDB; A7I199; -.
DR   SMR; A7I199; -.
DR   STRING; 360107.CHAB381_0710; -.
DR   EnsemblBacteria; ABS51738; ABS51738; CHAB381_0710.
DR   KEGG; cha:CHAB381_0710; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_7; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000002407; 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..640
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345250"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         289..303
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   640 AA;  71354 MW;  18479ECFEA0E1878 CRC64;
     MQYDIIVIGG GHAGIEACLA AARMGAKTLL ITILAEQIGA ASCNPAIGGL AKGHLVKEID
     ALGGQMGVCT DFAGIQFRTL NESKGPAVRG SRAQIDMDRY RIFMRNVLLN TSNLNISQEI
     ATEILTENDQ ITGVKTHLGN VYETNRLIIT TGTFLNGLIH VGENKLSAGR VGEFPSIRLS
     QSLKNLGLKM GRLKTGTCPR VDAKTIDFSA LELQNGDAQA HPFSFKTRFF ANEIEKFTKN
     LSKNFDENGN FNPTQIPCYI TYTNEKTHEI IRNNFDRAPL FTGQIHGIGP RYCPSIEDKI
     NKFADRDRHH VFVEPQTAEA SEYYLNGLST SLPYDVQVEF LHSVKGFENA KIVRHGYAIE
     YDFVEPTELK HSLETKKING LYLAGQINGT TGYEEAAAQG LIAGINAALD IQNKAPLILR
     RDEAYIGVLI DDLVTKGTKE PYRMFTSRAE FRLLLREDNA IFRLSGYGHD IGLIKDYEFD
     EISRRKAQIQ KGINFLLNNV ITPNKENLAK LKSLGADAIS QNTTWQKIVG GKNFSAEKIR
     EIDSMFVDFS DDELSEILTE CKYYFYIQMQ KDEVAKMKNM LNTKIPTELD FSKISGLSNE
     IIEKLNKFNP PTLFAASEIS GVTPAAIDIL HIYIKQFKGK