MNMG_PSEPG
ID MNMG_PSEPG Reviewed; 630 AA.
AC B0KRB9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=PputGB1_5442;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-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; CP000926; ABZ01324.1; -; Genomic_DNA.
DR RefSeq; WP_012274915.1; NC_010322.1.
DR AlphaFoldDB; B0KRB9; -.
DR SMR; B0KRB9; -.
DR STRING; 76869.PputGB1_5442; -.
DR EnsemblBacteria; ABZ01324; ABZ01324; PputGB1_5442.
DR KEGG; ppg:PputGB1_5442; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000002157; 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; tRNA processing.
FT CHAIN 1..630
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000076326"
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; 69413 MW; D24287A5D18DF8A4 CRC64;
MDFPSRFEVI 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 DSHQVFIEPE
GLTTHELYPN GISTSLPFDV QLELVRSIRG MENAHIVRPG YAIEYDYFDP RDLKYSLETK
VIGGLFFAGQ INGTTGYEEA GAQGLLAGTN AALRAQGRDS WCPRRDEAYI GVLVDDLITL
GTQEPYRMFT SRAEYRLILR EDNADLRLTE KGRELGLIDD QRWAAFCAKR DGIEREEQRL
KSTWVRPNTE QGQAIVDKFG TPLSHEYSLL NLLARPEIDY AGLIEATGGE AIDPQVAEQV
EIRTKYAGYI DRQQDEIARL RASEDTRLPV DIDYSTISGL SKEIQGKLGQ TRPETLGQAS
RIPGVTPAAI SLLLIHLKKR GAGRELEQSA