ID   MNMG_SYNJA              Reviewed;         643 AA.
AC   Q2JXG8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=CYA_0296;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABC98518.1; -; Genomic_DNA.
DR   RefSeq; WP_011429207.1; NC_007775.1.
DR   AlphaFoldDB; Q2JXG8; -.
DR   SMR; Q2JXG8; -.
DR   STRING; 321327.CYA_0296; -.
DR   PRIDE; Q2JXG8; -.
DR   EnsemblBacteria; ABC98518; ABC98518; CYA_0296.
DR   KEGG; cya:CYA_0296; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000008818; 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..643
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345346"
FT   BINDING         21..26
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         282..296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   643 AA;  71574 MW;  B3DB728DB1F92F74 CRC64;
     MLKVGRDNVD FLDHYDVIVV GGGHAGCEAA LAAARLGCNT LMLTLNLDKI AWQPCNPAVG
     GPAKSQLVHE IDALGGEMGK VTDRTYLQKR VLNRSRGPAV WALRAQTDKR EYARVMRSVV
     ENQPNLSIRE GTVTDLVLGR NDEVVGVVTH FGSVFGCGAV ILTTGTFLGG RIWIGRHWQP
     AGRAGEFAVE GLTDTLRQLG FETGRLKTGT PARVDRRSVD FSVMERQPGD PDLRWFSFDP
     EVWVPREQMD CYLTRTTPET HRIIRENLHE TPVYGGWVEA KGPRYCPSIE DKIVRFADKE
     SHQIFIEPEG RDLPELYIQG FSTGMPEKIQ IQMLRSLPGL ERCVMLRPAY AVEYDYLPAT
     QLYPTLMTKK VQGLFCAGQI NGTTGYEEAA AQGLIAGINA ARLVQGKPLV TLPRESSYIG
     TLIDDLCTKE LREPYRMLTS RSEYRLILRA DNADQRLTPL GREWGLIDDR RWALFQAKQA
     RIAAEIERLE TQRVKAHDPA GIHLSQLTGQ GIKGSATLAE LLRRNPIHYA DLLELGLGNE
     ELDPFEQEAA EIAVKYSGYI QRQQAQIEQV SKQYHRPLPP DLDYHSIPTL SKESREKLAA
     VRPLTVGQAA RIGGVNPADI NALLIYLEVR QRQKTAAAAP VGA