ID   MNMG_SYNR3              Reviewed;         643 AA.
AC   A5GWP3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=SynRCC307_2399;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-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; CT978603; CAK29302.1; -; Genomic_DNA.
DR   RefSeq; WP_011936811.1; NC_009482.1.
DR   AlphaFoldDB; A5GWP3; -.
DR   SMR; A5GWP3; -.
DR   STRING; 316278.SynRCC307_2399; -.
DR   EnsemblBacteria; CAK29302; CAK29302; SynRCC307_2399.
DR   KEGG; syr:SynRCC307_2399; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001115; 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; Reference proteome; tRNA processing.
FT   CHAIN           1..643
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016700"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         283..297
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   643 AA;  70351 MW;  0E4366653851D98D CRC64;
     MEPAALPTES FELIVVGGGH AGCEAALTAA RLGISTALFS LNLDRIAWQP CNPAVGGPAK
     SQLVHEVDAL GGVIGRLADA TALQKRVLNA SRGPAVWALR AQTDKRQYAR QMLQLLQHTP
     NLALREAMVT GLETSGSAES GDLRITGVRT YFGSIYNAQA VVLTTGTFLG GRIWVGNQSM
     PAGRAGEQPA EGLTEALQAL GFATDRLKTG TPARVDRRSV ALETLEEQPS DAHERWFSFD
     PEAWVSSEPM SCHITRTTAA THQLIKDNLH LTPIYGGFID SKGPRYCPSI EDKIVRFADK
     DSHQIFLEPE GRDTPELYIQ GFSTGLPERL QLKLLRTLPG LEQCVMLRPA YNVEYDYLPA
     TQLLPSLQTK RVAGLFSAGQ LNGTTGYEEA AAQGLVAGLN AVRLIRGQTP VHFPREGSYI
     GTLIDDLVTK DLREPYRVLT SRSEYRLVLR GDNADRRLTP LARELGLIDA RRWQIYERKQ
     EGIAAETKRL ETVRLKVSDP VAPAVVEQTG AAIKGSITLA DLLRRPGFHS NDLVRHGLAD
     GELPVDVREG AEIDVKYSGY LARQTQQIER VQRQGQRLIP SGIDFYSITT LSREARERLT
     AAQPLNLGQA SRLPGVSPAD VTALLLWLEL QDRQAATTTL ARP