ID   MNMG_SYNPW              Reviewed;         659 AA.
AC   A5GPI1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=SynWH7803_2420;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
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; CT971583; CAK24846.1; -; Genomic_DNA.
DR   RefSeq; WP_011934306.1; NC_009481.1.
DR   AlphaFoldDB; A5GPI1; -.
DR   SMR; A5GPI1; -.
DR   STRING; 32051.SynWH7803_2420; -.
DR   EnsemblBacteria; CAK24846; CAK24846; SynWH7803_2420.
DR   KEGG; syx:SynWH7803_2420; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_3; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001566; 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..659
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345347"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         293..307
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   659 AA;  71979 MW;  16EA3D5691604414 CRC64;
     MANSFSPTEI FDVIVVGGGH AGCEAAITSA RLGLNTALFT LNLDRIAWQP CNPAVGGPAK
     SQLVHEVDAL GGVIGRLADA TAIQKRILNA SRGPAVWALR AQTDKRQYSR QMLQLLQHTP
     NLALREAMVT GLEIDGDPAG GGEHWDPSQG PAARITGVRT YFGSLYGAKA VVLTAGTFLG
     GRIWVGHQSM AAGRAGEQAA EGLTEALQQL GFHTDRLKTG TPARVDRRSI ALDQLEEQPS
     DAADRFFSFD PAAWSSGEQM SCHITRTTAA THQLIKDNLH LTAIYGGVID SKGPRYCPSI
     EDKIVRFADK DSHQIFLEPE GRDTPEIYVQ GFSTGLPEPI QLQLLRSLPG LEQAVMLRPA
     YSVDYDYLPA TQLLPSLETK RVQGLFSAGQ LNGTTGYEEA AAQGLVAGLN AARRIRAEEA
     VHFPREGSYI GTMIDDLVSK DLREPYRVLT SRSEYRLVLR GDNADRRLTP LGRELGLIDD
     RRWRLFEDKL QAMEAEKQRL EQQRLKVSDP AAPAVEQETG APIKGSITLA DLLRRPGMHA
     ADLVRHGLAD AGLPLPVREG AEIDIKYSGY LARQQQQIDQ VKRQGRRKLP ETIDYASIST
     LSREAREKLT AVRPLTLGQA SQIPGVSQAD LTSLLMWLEL QQRRSQPSAS HLAPTGQAR