ID   MNMG_THEVB              Reviewed;         637 AA.
AC   Q8DLF8;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=tlr0535;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC08087.1; -; Genomic_DNA.
DR   RefSeq; NP_681325.1; NC_004113.1.
DR   RefSeq; WP_011056385.1; NC_004113.1.
DR   AlphaFoldDB; Q8DLF8; -.
DR   SMR; Q8DLF8; -.
DR   STRING; 197221.22294256; -.
DR   PRIDE; Q8DLF8; -.
DR   EnsemblBacteria; BAC08087; BAC08087; BAC08087.
DR   KEGG; tel:tlr0535; -.
DR   PATRIC; fig|197221.4.peg.564; -.
DR   eggNOG; COG0445; Bacteria.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000440; 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..637
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000117196"
FT   BINDING         17..22
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         278..292
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   637 AA;  70957 MW;  6CB17684D8F1FA9C CRC64;
     MSTLPAFQDE FDVIVVGAGH AGCEAALATA RLGCRTLLLT LNLDKIAWQP CNPAVGGPAK
     SQLVHEVDAL GGEIGRVSDR TYVQKRLLNA SRGPAVWALR AQTDKREYSA VMKQVVENQP
     NLLVREGMVT DLVLDANDTV IGVETYFGVA FRCQAVILTT GTFLGGRIWV GNKSMPAGRA
     GEFAAEGLSQ TLARLGFEVD RLKTGTPARV DRRSVDYSKM EPQPPDEQVR WFSFDPTVWV
     ERPQMNCYLT RTTPETHRLI REHLHLTPVY GGWVDAKGPR YCPSIEDKIV RFADKESHQI
     FIEPEGRNTP ELYIQGFSTG LPEPLQLQLL RTLPGLENCI MLRPAYAVEY DYLPATQCFP
     TLMTKKIQGL FCAGQINGTT GYEEAAAQGI VAGINAARFV QRKPMITFPR QESYIGTLID
     DLCTKELREP YRMLTSRSEY RLVLRSDNAD QRLTPLGYEI GLVSEAQWQV FQAKQRRLAA
     ETQRLQTTRI KAHEPVGEAI VTATGQAIKS AIALEELLRR SGVHYELLDR HGLGNPDLTP
     QEKEAVEIAI KYAGYIERQQ REIEQIARQE QRPLPVDLDY FAIPTLSMEA REKLSAIRPL
     TIGQASRIGG VNPADINALL VYLQVQQQRQ SLTAVGG