MNMG_SINMW
ID MNMG_SINMW Reviewed; 623 AA.
AC A6UEE8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Smed_3204;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-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; CP000738; ABR62028.1; -; Genomic_DNA.
DR RefSeq; WP_012067409.1; NC_009636.1.
DR RefSeq; YP_001328863.1; NC_009636.1.
DR AlphaFoldDB; A6UEE8; -.
DR SMR; A6UEE8; -.
DR STRING; 366394.Smed_3204; -.
DR EnsemblBacteria; ABR62028; ABR62028; Smed_3204.
DR GeneID; 61610786; -.
DR KEGG; smd:Smed_3204; -.
DR PATRIC; fig|366394.8.peg.6442; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_5; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000001108; 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..623
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016682"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 623 AA; 67954 MW; 7DC93D6A19A6BB0A CRC64;
MADYDVIVIG GGHAGCEAAA ASARLGARTL LITHKKDTIG VMSCNPAIGG LGKGHLVREI
DALDGLMGRV ADAAGIQFRL LNRRKGPAVR GPRTQADRKL YREAMQREIA SIENLDVAEG
DAFDLQTEDG VVCGAVMKDG RSFRAASVVL TTGTFLRGLI HIGDRKMPAG RVGEQPSVGL
SETLARFGLQ LGRLKTGTPA RLDGRTIDWG RVGRQGPDEN PVPFSFMTDA IVNRQIDCGV
TRTTDATHKI IADNIHRSAM YSGQIEGVGP RYCPSIEDKI VRFGERDGHQ IFLEPEGLDD
DTVYPNGIST SLPEDVQDAF IRTIPGLEQV TILQPGYAIE YDHVDPRELE PSLGVRRMPG
LFLAGQINGT TGYEEAGAQG LVAGLNAALR AAERAPFFFS RTDSYIGVMI DDLTSRGIAE
PYRMFTSRAE YRLSLRADNA DMRLTPVGIE LGCVGNARLT RFQQWKSAYE AGRTLLQSLS
VTPNEGKRFG LKLNQDGQRR TAFEILSYPD QSIEGLRPLW PELQAIATDV AAALEIDAAY
AVYMERQAAD IIGVQREEST AIPEAFDYES LPGLSNELKQ KLAQQKPRNL SQAMKVDGVT
PAAISLILSW LRREDRRSKR VGG