MNMG_PSEP1
ID MNMG_PSEP1 Reviewed; 630 AA.
AC A5WBB4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-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=Pput_5306;
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) 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; CP000712; ABQ81424.1; -; Genomic_DNA.
DR RefSeq; WP_012054153.1; NC_009512.1.
DR AlphaFoldDB; A5WBB4; -.
DR SMR; A5WBB4; -.
DR STRING; 351746.Pput_5306; -.
DR EnsemblBacteria; ABQ81424; ABQ81424; Pput_5306.
DR KEGG; ppf:Pput_5306; -.
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_1000016648"
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; 69459 MW; FAA56471245CE5AD CRC64;
MDFPSRFDVI VIGGGHAGTE AALASARMGV KTLLLTHNVE TLGHMSCNPA IGGIGKSHLV
KEIDALGGAM ALATDKSGIQ FRVLNNRKGP AVRATRAQAD RAIYKAVVRE ILENQPNLWI
FQQSCDDLIV EQDQVKGVVT QMGLRFFAES VVLTTGTFLG GLIHIGLQNH SGGRAGDPPS
IALAHRMREL PLRVGRLKTG TPPRIDGRSV DFSVMTEQPG DTPIPVMSFM GNAEMHPRQV
SCWITHTNAR THEIIASNLD RSPMYSGVIE GVGPRYCPSI EDKIHRFADK ESHQVFIEPE
GLNTHELYPN GISTSLPFDV QLELVRSIRG MENAHIVRPG YAIEYDYFDP RDLKYSLETK
VIGGLFFAGQ INGTTGYEEA GAQGLLAGTN AALRAQGRDS WCPRRDEAYI GVLVDDLITL
GTQEPYRMFT SRAEYRLILR EDNADLRLTE KGRELGLIDD LRWAAFCAKR DGIEREEQRL
KSTWVRPNTE QGQAVVDKFG TPLSHEYSLL NLLARPEIDY AGLIEATGGE AIDPQVAEQV
EIRTKYAGYI DRQQDEIARL RASEDTRLPV DIDYTTISGL SKEIQGKLSQ TRPETLGQAS
RIPGVTPAAI SLMLIHLKKR GAGRELEQSA