MNMG_VIBCM
ID MNMG_VIBCM Reviewed; 631 AA.
AC C3LSK0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=VCM66_2695;
OS Vibrio cholerae serotype O1 (strain M66-2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M66-2;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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; CP001233; ACP06987.1; -; Genomic_DNA.
DR RefSeq; WP_000965608.1; NC_012578.1.
DR AlphaFoldDB; C3LSK0; -.
DR SMR; C3LSK0; -.
DR EnsemblBacteria; ACP06987; ACP06987; VCM66_2695.
DR KEGG; vcm:VCM66_2695; -.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000001217; Chromosome I.
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..631
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000122758"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 180
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"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 631 AA; 70172 MW; AD9E84CCB38D3729 CRC64;
MLYHETFDVI VVGGGHAGTE AALAAARTGQ RTLLLTHNID TLGQMSCNPA IGGIGKGHLV
KEVDAMGGLM AQAIDHAGIQ FRTLNASKGP AVRATRAQAD RALYKAYVRN VLENTPNLTL
FQQAVDDVIV EHDHIRGVVT QMGLKFHAKA VVLTVGTFLG GKIHIGLENY AGGRAGDPPS
IALAHRLREL PFRVDRLKTG TPPRIDANSV DFSVLEAQHG DNPTPVFSFM GKREHHPRQI
PCYITHTNER THDVIRANLD RSPMYAGIIE GIGPRYCPSI EDKVMRFADK DSHQIFIEPE
GLTTTELYPN GISTSLPFDV QVQIVRSMKG FENAHIVRPG YAIEYDFFDP RDLKQTYETK
YIHGLFFAGQ INGTTGYEEA AAQGLMAGLN ASLYSQDKEG WSPRRDQAYM GVLIDDLSTM
GTKEPYRMFT SRAEYRLLLR EDNADLRLTE KARELGLVDD ARWARFNQKI DNMAKERQRL
QETWMNPNSV GVEQLNTLLK TPMSREASGE DLLRRPEMTY ELLTTLPAFA PALEDAEAAE
QVEIQVKYDG YIQRQQDEIE KSLRHEHTKL PAELDYKQVK GLSNEVVLKL NAAKPETIGI
ASRISGITPA AISILLVHLK KHGMLKKGEA A