ID   MNMG_SYNE7              Reviewed;         635 AA.
AC   Q31KG6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, 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=Synpcc7942_2423;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB58453.1; -; Genomic_DNA.
DR   RefSeq; WP_011378455.1; NC_007604.1.
DR   AlphaFoldDB; Q31KG6; -.
DR   SMR; Q31KG6; -.
DR   STRING; 1140.Synpcc7942_2423; -.
DR   PRIDE; Q31KG6; -.
DR   EnsemblBacteria; ABB58453; ABB58453; Synpcc7942_2423.
DR   KEGG; syf:Synpcc7942_2423; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2423-MON; -.
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..635
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016699"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         274..288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   635 AA;  70424 MW;  D8079AF6A15FE517 CRC64;
     MPHTEEFDVI VIGAGHAGCE AALAAARLGC QTLLLTLNLD RIGWQPCNPA VGGPAKSQLA
     HEVDALGGEI GKMADRTYLQ KRVLNASRGP AVWALRAQTD KREYAAVIKQ VLEQQPNLRL
     REGMVTDLLI GPNDEVQGVT TYFGSSFRAK AVILTTGTFL GGCIWVGNKS MPAGRAGEFA
     AVGLTETLQR LGFETDRLKT GTPARVDKRS VDYSRLEPQP GDPEVRWFSF DPEAWVEREQ
     LPCYLTRTTA ETHKLIRDNL HLTPVYGGYI DAKGPRYCPS IEDKIVRFAD KESHQIFIEP
     EGRDIPELYI QGFSTGLPED LQLALLQTLP GLEDCVMLRP AYAVEYDYLP ATQCLPTLMT
     RRVEGLFSAG QLNGTTGYEE AAAQGIVAGI NAARFVQGQD AIVFPREGSY IGTLIDDLCT
     KDLREPYRVL TSRSEYRLLL RADNADQRMT PLGREIGLID DRRWALFEQK QARIAAEQTR
     LTQQRVKEHD PVGQAIAQQT QAPIKGSATL ADLLRRPNFH YIDLEAHGLG DPSLAIAEKE
     GAEIAIKYAG YLQRQQAQVD QVVRQSQRPL PVDLDYSAIT SMRLEAREKL ARFRPLTLGQ
     ASRIGGVNPA DINALLIWLE VQERQRSQVE TALVR