MNMG_XANCB
ID MNMG_XANCB Reviewed; 634 AA.
AC B0RMP9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, 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=xcc-b100_0403;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP49734.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RMP9; -.
DR SMR; B0RMP9; -.
DR KEGG; xca:xcc-b100_0403; -.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000001188; 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..634
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345359"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 279..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 634 AA; 68917 MW; F0476ECBC8E2DBA1 CRC64;
MSDSFYRYDV IVIGGGHAGT EAALAAARAG ARTLLLTHNI ETVGAMSCNP AIGGIGKGHL
VKEIDALGGA MAKAADLAGI QWRTLNASKG PAVRATRCQA DRNLYRSAIR RIVEAQPNLT
VFQAAVDDLI IHNGAAEGDS VRGVITQTGL RFEATAVVLT AGTFLAGKIH VGETQYAAGR
MGDPPATTLA ARLRERPFAI DRLKTGTPPR IDGRTLDYTM MDEQPGDDPL PVMSFMGQVS
DHPTQVSCWI THTTEQTHDI IRGALHRSPL YSGQIEGIGP RYCPSIEDKV VRFADKTSHQ
IFVEPEGLDV TEIYPNGIST SLPFDVQLAL VRSIRGFAQA HITRPGYAIE YDFFDPRGLK
ASLETKAVGG LFFAGQINGT TGYEEAAAQG LLAGLNAARH VQALPAWSPR RDEAYLGVLV
DDLITHGTTE PYRMFTSRAE YRLQLREDNA DLRLTGVGRA MGLVDDARWA RFSSKQEAVQ
RETARLSALW ATPGNALGRE VVDTLGVPMS RETNVLDLIK RPELSYAALM RVPTLGPGVD
DAQVAEQVEI GVKYAGYLDR QRDEIARQQR HETTPIPEGF DYAGVRGLSM EVQQKLERVR
PQSIGQAQRI PGMTPAAISL LLVHLERARR SQVA