MNMG_DEIRA
ID MNMG_DEIRA Reviewed; 600 AA.
AC Q9RYC3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=DR_0027;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF09619.1; -; Genomic_DNA.
DR PIR; D75569; D75569.
DR RefSeq; NP_293753.1; NC_001263.1.
DR RefSeq; WP_010886675.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RYC3; -.
DR SMR; Q9RYC3; -.
DR STRING; 243230.DR_0027; -.
DR PRIDE; Q9RYC3; -.
DR EnsemblBacteria; AAF09619; AAF09619; DR_0027.
DR KEGG; dra:DR_0027; -.
DR PATRIC; fig|243230.17.peg.192; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_0; -.
DR InParanoid; Q9RYC3; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
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 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..600
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117092"
FT REGION 216..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 267..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 600 AA; 65260 MW; CDBDACFC19768EDA CRC64;
MKGWNVIVIG GGHAGLEAAW AAAKFSRVAL LVGNPATVGR MPCNPAVGGP GKSQLVFEVQ
ALGGLMGRLA DDTAIHTRML NASKGPAVQS LRVQNERDAY AERAQDVIFG HSEIEIVRGE
AADLEQDGQG GWVVVTSDGR RLHARSVVLA AGTFMRGVTW YGRQSRPEGR QGEPPSRFLS
APLERGGHVL KRYKTGTPPR VRADSVRFAD LLEIPADPQP RGFTGTPGPR AAESPTWQTH
TTPQTHALIQ ENLHESPMYA GDIEGLGPRY CPSIEDKVVK FAHHDRHLLF VEPDGVQTSE
VYLQGFSSSL PPRLQDELVR TLPGFEQAVI QRYAYAVEYD VVDSTELTLN LESKKLPGLF
TAGQLNGTSG YEEAAAQGLV AGTAAARRSL GLDEQVIGRE TSYLGVLLDD LVFKGSDEPY
RMMTSRVEHR LLVRQDNADE RMTPIGHALG LVDDAELIRV QEKYARVQSG IKSLSKQRMQ
GQTADAWLRR PELSLADVET LGATLPAELG ASEREAVEIR VKYAGYIARA ESQLRSEAKA
RELSLSGVNF AGITALSNEA REKLTRLQPQ TVEQASRISG VRHADISALL VHLKGQRVGS
