ID   MNMG_CAMJJ              Reviewed;         619 AA.
AC   A1W0H2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=CJJ81176_1203;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-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; CP000538; EAQ72269.1; -; Genomic_DNA.
DR   RefSeq; WP_002864546.1; NC_008787.1.
DR   AlphaFoldDB; A1W0H2; -.
DR   SMR; A1W0H2; -.
DR   STRING; 354242.CJJ81176_1203; -.
DR   PRIDE; A1W0H2; -.
DR   EnsemblBacteria; EAQ72269; EAQ72269; CJJ81176_1203.
DR   KEGG; cjj:CJJ81176_1203; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_7; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000000646; 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..619
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016575"
FT   BINDING         8..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         267..281
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   619 AA;  69172 MW;  18261C2019852AE2 CRC64;
     MFDVIVIGGG HAGVEASAAA ARMGKKTLLL TTLIEQIGAA SCNPAIGGLA KGHLVKELDA
     MGGLMGEITD EAGIQFRILN ESKGVAVQGS RAQIDMDKYR IIARNKLLKL PNLEISQEQA
     SVLIVENDEV KGVKTNLENI YFAKKVILTT GTFLNGLIHV GENKLQAGRV GELASVNLGN
     YLQTLGLKMG RLKTGTCPRV DAKSIDFSVL EIQDGDVNPK AFSFRSRNFN PTQLPCYIAR
     TNTTTHEIIK NNFYRAPLFT GQIEGVGPRY CPSIEDKINR FSDKESHHLF IEPQTIDATE
     YYINGFSTSL PYEVQTQMLR SVEGFENAKI TRFGYAIEYD YIEPTELKHT LELKKIKNLY
     CAGQINGTTG YEEAAAQGFM AGINASLSID MKEPLILRRD EAYIGVLIDD LVVKGTKEPY
     RMFTSRAEFR LLLREENAIL RLGKYGYDLG LLSEQDFTYI QNIANNLQKG LEFLLSKEFT
     PNNQNNAFLE SLGEDKISSI VNLQKIVARA SFDIEKLKKL DPIFETMDHY SLREILNEAK
     YYHYISMQKA QVEKMKNLSE LKIPENFDFK SVSGLSNEVV EKLNHHKPPT IFAASQISGI
     TPAALDILQI YIKMQKKKA