ID   MNMG_CAMC1              Reviewed;         620 AA.
AC   A7ZBK0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Ccon26_02450; ORFNames=CCC13826_1922;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-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; CP000792; EAT97741.1; -; Genomic_DNA.
DR   RefSeq; WP_012001173.1; NC_009802.2.
DR   AlphaFoldDB; A7ZBK0; -.
DR   SMR; A7ZBK0; -.
DR   STRING; 360104.CCC13826_1922; -.
DR   EnsemblBacteria; EAT97741; EAT97741; CCC13826_1922.
DR   KEGG; cco:CCC13826_1922; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_7; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001121; 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..620
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345247"
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   620 AA;  69095 MW;  D5FCD19CE52335B3 CRC64;
     MDYEIIVVGG GHAGIEASLA AARMGKQTLL ITILAEQIGA ASCNPAIGGL AKGHLVKEID
     ALGGQMGLTT DAVGIQFRVL NESKGPAVRG SRAQIDMDRY RVYMRNLLLN TPNLEISQEI
     ATEILSENGE ITGVKTHLNN TYNAKKVIIT TGTFLNGLIH VGFNKLEAGR VGELSAKDLS
     SSLRELGLNL GRLKTGTCPR IDAKTINFEI LEKQDGDAKP VAFSFRTKNF SPTQLPCYIA
     YTNETTHEII RSNFDKAPLF TGQIEGIGPR YCPSIEDKIN RFGDRDRHHL FIEPQTLEAT
     EYYINGFSTS LPYEVQVQML RSVKGFENAK IVRHGYAIEY DYVEPTQLKH SLETKKVKGL
     YLAGQINGTT GYEEAGAQGL MAGINAALSL DNKEPLILRR DEAYIGVLID DLVTKGTKEP
     YRMFTSRAEY RLLLREENAI LRLGGYGHEL GLLDDETFNE IENIRRNLKE GLEFLNETQI
     TPSKANLELL ASLDEEPISQ NVSLQKIVAR KSFTAEKLRK LDERFVNLDD ASMDQILTEC
     KYQHYISEQK NQIEKMKDMM DVKIPENFDF RSISGLSNEV VEKLEKFAPP TLFAASEISG
     ITPAAIDILH IYIKMSEKKA