ID   MNMG_CHLPM              Reviewed;         621 AA.
AC   A4SC27;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Cvib_0007;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-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; CP000607; ABP36036.1; -; Genomic_DNA.
DR   RefSeq; WP_011889269.1; NC_009337.1.
DR   AlphaFoldDB; A4SC27; -.
DR   SMR; A4SC27; -.
DR   STRING; 290318.Cvib_0007; -.
DR   EnsemblBacteria; ABP36036; ABP36036; Cvib_0007.
DR   KEGG; pvi:Cvib_0007; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_10; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
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_1000076325"
FT   BINDING         8..13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         269..283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   621 AA;  68096 MW;  D2C6A89069A3392C CRC64;
     MYDIIVAGAG HAGCEAALAA ARSGSSCLLI SSDLTAVARM SCNPAIGGVA KGQITREIDA
     LGGEMAKAID ATGIQFRMLN LSKGPAMHSP RAQADRTAYT EYMKRVLEAE TNLDLLQDTV
     TGIEVRGGQF FGVELQSGRI LRAGAAILTC GTFLNGLIHI GMNHFPGGRT IAEPPVTGLT
     ESLVAAGFTT ARLKTGTPPR VDRRSIDYSI VIEQKGDENP PPFSFSSGSI AGKEQISCFL
     TKTTHKTHEI LRTGFDRSPL FSGKVQGVGP RYCPSIEDKI HRFTERDSHH IFLEPEGFHT
     NEMYVNGFST SLPEDIQIAG LQSIPGMEEV KMIRPGYAIE YDYFHPSQIR RSLETKAVEN
     LYFAGQINGT SGYEEAAAQG LMAGINASRK LKELPPIHLQ RSDAYIGVLI DDLVTKETNE
     PYRMFTSSAE HRLILRHDNA DLRLRKFGHT AGLVDDDTYR ETLSKDDEIV RMTAFLRSKT
     IPTTALYNLL PAESNRPMTG GQKAASALKR PGITLNRLFA ALPDFAKEAR LISSNPLVHE
     QVEINLAYEG YLKRELLQTE KVARLESLIL PETFNYHSVT GLSSEGREKL LHFRPETLGQ
     ASRIMGVSPS DISVLMVRLG R