ID   MNMG_CAMFF              Reviewed;         621 AA.
AC   A0RQV2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=CFF8240_1446;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) 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; CP000487; ABK82755.1; -; Genomic_DNA.
DR   RefSeq; WP_002850412.1; NC_008599.1.
DR   AlphaFoldDB; A0RQV2; -.
DR   SMR; A0RQV2; -.
DR   STRING; 360106.CFF8240_1446; -.
DR   EnsemblBacteria; ABK82755; ABK82755; CFF8240_1446.
DR   GeneID; 61065265; -.
DR   KEGG; cff:CFF8240_1446; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_7; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000760; 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; tRNA processing.
FT   CHAIN           1..621
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345249"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         268..282
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   621 AA;  69323 MW;  B9119C03038C1080 CRC64;
     MNYDVIVVGG GHAGIEASLA AAKMGAKTLL ITILAEQIGA ASCNPAIGGL AKGHLVKEID
     ALGGQMGLTT DACGIQFRLL NESKGPAVRG SRAQIDMDRY RVYMRNLLLN TPNLEVTQEI
     ATEILTKDNN IIGVKTHLDN NYGTKKLIIT TGTFLNGLIH VGFNKLEAGR VGELSSKSLS
     ASLKSLNLEM GRLKTGTCPR VLAKSIDFSV LERQDGDQDP TPFSFRTKEF NKTQLPCYIA
     YTNEKTHEII RSNFDRAPLF TGQIEGIGPR YCPSIEDKIN RFGDRERHHL FIEPQTREAT
     EYYINGFSTS LPYDAQVEML RSVKGFQNAK IVRHGYAIEY DYVSPTELKH TLETKKINGL
     YLAGQINGTT GYEEAAAQGL MAGINAALNL KTREPLILRR DESYIGVLID DLVTKGTKEP
     YRMFTSRAEY RLLLREDNAN LRLSKYGYNV GLLPKEAFEE MLKLKSNLEK GMEILLTKDM
     SPNKENLEFL ASIDEDIINE KVPLQKIAAR KSFTIEKLRK LNEFFLNLDD KSLNQILTEA
     KYYHYIAQQQ IEVEKMKGLL DIKIPKSLEF KSISGLSNEV VEKLNKFAPP TLAAASNISG
     ITPVAIDILH IAIKYHCQKT K