ID   MNMG_PSEPW              Reviewed;         630 AA.
AC   B1JFV2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=PputW619_5211;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA75686.1; -; Genomic_DNA.
DR   RefSeq; WP_012316954.1; NC_010501.1.
DR   AlphaFoldDB; B1JFV2; -.
DR   SMR; B1JFV2; -.
DR   STRING; 390235.PputW619_5211; -.
DR   PRIDE; B1JFV2; -.
DR   EnsemblBacteria; ACA75686; ACA75686; PputW619_5211.
DR   KEGG; ppw:PputW619_5211; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_6; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
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..630
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345319"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         273..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   630 AA;  69284 MW;  F46578180C1CCA60 CRC64;
     MDFPSRFEVI VIGGGHAGTE AALASARMGV KTLLLTHNVE TLGHMSCNPA IGGIGKSHLV
     KEIDALGGAM ALATDKSGIQ FRVLNNRKGP AVRATRAQAD RAIYKAVVRE ILENQPNLWI
     FQQSCDDLIV EQDQVKGVVT QMGLRFFADS VVLTTGTFLG GLIHIGLQNH SGGRAGDPPS
     IALAHRMREL PLRVGRLKTG TPPRIDGRSV DFSVMTEQPG DTPIPVMSFM GNAAMHPRQV
     SCWITHTNAR THEIIASNLD RSPMYSGVIE GVGPRYCPSI EDKIHRFADK ESHQVFIEPE
     GLTTHELYPN GISTSLPFDV QLELVRSIRG MENAHIVRPG YAIEYDYFDP RDLKYSLETK
     VIGGLFFAGQ INGTTGYEEA GAQGLLAGTN AALRAQGRES WCPRRDEAYI GVLVDDLITL
     GTQEPYRMFT SRAEYRLILR EDNADLRLTE KGRELGLIDD QRWAAFCAKR DGIEREEQRL
     KSTWVRPNTP QGQAVVDKFG TPLSHEYSLL NLLARPEVDY AGLIEATGGE QIDPQVAEQV
     EIKTKYAGYI DRQQDEIARL RASEDTCLPV DIDYTSISGL SKEIQGKLGQ TRPQTLGQAS
     RIPGVTPAAI SLLLIHLKKR GAGRELEQSA