ID   MNMG_NOSS1              Reviewed;         640 AA.
AC   Q8YR87;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=alr3561;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB75260.1; -; Genomic_DNA.
DR   PIR; AB2251; AB2251.
DR   RefSeq; WP_010997711.1; NZ_RSCN01000034.1.
DR   AlphaFoldDB; Q8YR87; -.
DR   SMR; Q8YR87; -.
DR   STRING; 103690.17132694; -.
DR   EnsemblBacteria; BAB75260; BAB75260; BAB75260.
DR   KEGG; ana:alr3561; -.
DR   eggNOG; COG0445; Bacteria.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000002483; 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   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..640
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117044"
FT   BINDING         19..24
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         280..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   640 AA;  71425 MW;  435D0E22B35796A7 CRC64;
     MTMHNSVEFQ DAFDVIVVGA GHSGCEAALA TARLGCRTLL LTLNLDKIAW QPCNPAVGGP
     AKSQLTHEVD ALGGEIGKMA DRTYLQKRIL NSSRGPAVWA LRAQTDKREY AAIMKNIVEN
     QENLSIRESM VTDLVLGAND EVIGVETYFG VAFQCKAVIL TTGTFLGGKI WVGNKSMPAG
     RAGEFAAEGL TETLNRLGFE TGRLKTGTPA RVDKRSVDYS KMQLQPGDAE VRWFSFDPDV
     WVEREQLPCH MTRTTPETHR LIRENLHLSP VYGGWVEAKG PRYCPSIEDK IVRFVDKESH
     QIFIEPEGRD IPELYIQGFS TGLPENLQLQ MLRSLPGLEN CVMLRPAYAV EYDYLPATQC
     YPTLMTKKIA GLFCAGQVNG TTGYEEAAAQ GIVAGINAAR FVRDEEMIVF PREHSYLGTL
     VDDLCTKDLR EPYRMLTSRS EYRLLLRSDN ADQRLTPLGR EIGLIDDRRW QMFTRKQEQI
     TGEKERLYAT RVKENDDVGK AIASNTQQAI KGSITLADLL RRPGFHYVDL DRYGLGNPEL
     TPAEKEGAEI DIKYSGYLAR QQSQIEQIAR QAQRQLPGDL DYTTVDTLSK EAREKLNKVK
     PLTIGQAARI GGVNPADINA LLIYLELRQS KHQKGLAVLP