ID   MNMG_GLOVI              Reviewed;         656 AA.
AC   Q7NM86;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
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}; OrderedLocusNames=gll0881;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC88822.1; -; Genomic_DNA.
DR   RefSeq; NP_923827.1; NC_005125.1.
DR   AlphaFoldDB; Q7NM86; -.
DR   SMR; Q7NM86; -.
DR   STRING; 251221.35211444; -.
DR   PRIDE; Q7NM86; -.
DR   EnsemblBacteria; BAC88822; BAC88822; BAC88822.
DR   KEGG; gvi:gll0881; -.
DR   PATRIC; fig|251221.4.peg.899; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   InParanoid; Q7NM86; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   PhylomeDB; Q7NM86; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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..656
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345275"
FT   BINDING         44..49
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         305..319
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   656 AA;  72592 MW;  96D185852A1BCAE9 CRC64;
     MSCLPDWLAA GCRDGDAASH PTIRLRFRTA TVHYLAEFDV VVVGAGHSGC EAALAAARLG
     CRTLLVTMNL DTIAWQPCNP AVGGPAKSQL VHEVDALGGE MAKITDRTYL QKRVLNSSRG
     PAVWALRAQT DKREYARELK QVLEATPNLT LRQGQITDIH LGPHDEICGV GTFFDVHFAC
     RAVILTTGTF LGGRIWIGRK SMSAGRAGEF AAEGLTATLE RLGFETGRLK TGTPARVDRR
     TVDFGVMEVQ PPDPELRWFS FDPRAWVERE QLNCYLTRTT AATHQVIRDH LHLSPMYSGD
     IEARGPRYCP SIEDKIVRFA DKESHQIFIE PEGRDTPELY VQGFSTSLPE TVQIAMLRTL
     PGLEACAVLR PAYAVEYDYL PATQCYATLM TKRVEGLFCA GQINGTTGYE EAAAQGIVAG
     INAARLVRGE ALVILPREGS YIGTLIDDLV TKEIREPYRM LTSRSEYRLV LRSDNADRRL
     TPLGREIGLV DDERWGLYQK KIAAITCERQ RLETTRLNAR DLPVHLAAKP GSITLADLLR
     RPGLHYGDLE SLNQGVLLDA QVREGVEIEV KYSGYIERQN EQIERVSAQH ARVIPADLDY
     ERLSTLSKES REKLNRIRPR TIGQAGRIGG VNPADVSALL VYLELAQAGR LTPAAP