MNMG_THIDA
ID MNMG_THIDA Reviewed; 632 AA.
AC Q3SF55;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Tbd_2808;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ98761.1; -; Genomic_DNA.
DR RefSeq; WP_011313320.1; NC_007404.1.
DR AlphaFoldDB; Q3SF55; -.
DR SMR; Q3SF55; -.
DR STRING; 292415.Tbd_2808; -.
DR EnsemblBacteria; AAZ98761; AAZ98761; Tbd_2808.
DR KEGG; tbd:Tbd_2808; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000008291; 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; Reference proteome; tRNA processing.
FT CHAIN 1..632
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016705"
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 632 AA; 68746 MW; 63676DF51FC1FD0E CRC64;
MKFPESFDVI VVGGGHAGTE AALAAARMGA KTLLLTHNIE TLGAMSCNPS IGGIGKGHLV
REVDALGGAM ALATDEAGIQ FRTLNSSKGP AVRATRAQAD RVLYKAAIRQ RLENQPGLTL
FQQAVDDLVL DGARVVGVKT QLGILFEARA VVLTAGTFLA GLVHVGLENF QAGRMGDPPA
VSLAARLREL DLPVGRLKTG TPPRIDGRTI DYSRTQVQPG DDPAPVFSFM GDRSMHPAQR
PCWITHTTVA THEIIRGGLD RSPLYAGVIE GVGPRYCPSI EDKITRFADK ASHQIFLEPE
GLTTHEIYPN GISTSLPFDV QHAIVRSIPG LEHAHILRPG YAIEYDYYDP RNLKASLETK
SIAGLFFAGQ INGTTGYEEA AAQGLLAGLN AALQTQGKDA WSPGRHEAYL GVLVDDLITR
GVSEPYRMFT SRAEYRLQLR EDNADMRLTE TGRALGVVDD ARWDQFNRKR DEVARETERL
KSVWVNPAIL PADAATQLIG QPIEREYSLF DLLRRPNLGY AQVLALPGGG AGVADVGVAE
QVEIAAKYQG YIDRQNEEVD KHREQEGLRL PPDLDYTRLT GLSMEVRQRL QTAQPETLGQ
ASRLQGVTPA AISVLLVYAK RGFKPDEQKK SA