MNMG_UREU1
ID MNMG_UREU1 Reviewed; 614 AA.
AC B5ZAL6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-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=UUR10_0043;
OS Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=565575;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33699 / Western;
RA Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL Submitted (OCT-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; CP001184; ACI59879.1; -; Genomic_DNA.
DR RefSeq; WP_004025657.1; NC_011374.1.
DR AlphaFoldDB; B5ZAL6; -.
DR SMR; B5ZAL6; -.
DR STRING; 565575.UUR10_0043; -.
DR EnsemblBacteria; ACI59879; ACI59879; UUR10_0043.
DR GeneID; 45015598; -.
DR KEGG; uue:UUR10_0043; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_14; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000002018; 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..614
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000095669"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 271..285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 614 AA; 69112 MW; A6636ACE6A88EC54 CRC64;
MKKYDVIVIG AGHAGLEAAF ATSNLNLQTA LITLDEKGIG MMPCNPSIGG PAKGIVTREI
DALGGIQGKA ADATTMQMKI LNSSKGPGVW AIRAQIDKIA YQRWFKQQIK QQKNLDLIIA
EVSDLLVENN IVKGVILSDQ KIIQADYVII TTGTYLKSIT HRGSVCVDEG ADGTKNAKFL
SDVLVKLGFE LIRLKTGTPA RIKKDSIDFT NMVLEPGTNQ KIAFSHYHPV YKPYDKQLPC
HIIYTNEQTH QIIRENLNKS AMYGGMISGI GPRYCPSIED KIVKFSEKPR HQIFVEPESY
ELDSMYLGGF STSMPIDVQE KMIRSLPGLE DCEILKYAYA IEYDAIDPTQ LYPSLESKLV
NNLFFAGQIN GTSGYEEAAA QGLMAAINVS QKHKNKEPIV LGRDQAYIGV MIDDIVTKGV
VEPYRLLTSR AEHRLALRND NADDRLMKIG FEIGLLKPEV YDQYLNNLKQ INEVLNWLKT
TTVGQIDDLK FTTLKTNSYL IDYLKRPEVK LNDLLIYCPI KIEDEQIINK VQIQVKFEGY
IKNQEENLKQ LKRLNNIKLH GIVDYKEVPN ISLETIDKLN KIKPLDLEQA SRISGVNLTD
IAMIKYYLER IKND