MNMG_PSEPU
ID MNMG_PSEPU Reviewed; 630 AA.
AC P25756;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TN2100;
RX PubMed=1552862; DOI=10.1111/j.1365-2958.1992.tb01510.x;
RA Ogasawara N., Yoshikawa H.;
RT "Genes and their organization in the replication origin region of the
RT bacterial chromosome.";
RL Mol. Microbiol. 6:629-634(1992).
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; X62540; CAA44419.1; -; Genomic_DNA.
DR PIR; JQ1223; BWPSAP.
DR AlphaFoldDB; P25756; -.
DR SMR; P25756; -.
DR STRING; 1240350.AMZE01000066_gene3189; -.
DR eggNOG; COG0445; Bacteria.
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_0000117155"
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; 69496 MW; 03B86C228F413E7C CRC64;
MDFPSRFDVI VIGGGHAGTE AALASARMGV KTLLLTHNVE TLGHMSCNPA IGGIGKSHLV
KEIDALGGAM ALATDKSGIQ FRVLNNRKGP AVRATRAQAD RAIYKAVVRE ILENQPNLWI
FQQNCDDLIV 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 QRWAAFCAKR DGIEREEQRL
KSTWVRPNTE QGQAIVDKFG TPLSHEYSLL NLLARPEIDY AGLIEATGGE AIDPQVAEQV
EIRTKYAGYI DRQQDEIARL RASEDTRLPV DIDYTTISGL SKEIQGKLSQ TRPQTLGQAS
RIPGVTPAAI SLLLIHLKKR GAGRELEQSA
