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Database: UniProt
Entry: Q5KU58
LinkDB: Q5KU58
Original site: Q5KU58 
ID   MNMG_GEOKA              Reviewed;         629 AA.
AC   Q5KU58;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   14-MAY-2014, entry version 65.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=GK3493;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of
RT   thermophilic Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
CC   -!- FUNCTION: NAD-binding protein involved in the addition of a
CC       carboxymethylaminomethyl (cmnm) group at the wobble position (U34)
CC       of certain tRNAs, forming tRNA-cmnm(5)s(2)U34 (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Heterotetramer of two MnmE and
CC       two MnmG subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MnmG family.
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DR   EMBL; BA000043; BAD77778.1; -; Genomic_DNA.
DR   RefSeq; YP_149346.1; NC_006510.1.
DR   ProteinModelPortal; Q5KU58; -.
DR   STRING; 235909.GK3493; -.
DR   EnsemblBacteria; BAD77778; BAD77778; GK3493.
DR   GeneID; 3185612; -.
DR   KEGG; gka:GK3493; -.
DR   PATRIC; 21968593; VBIGeoKau81518_3726.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; HTNEQTH; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; GKAU235909:GJO7-3606-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR004416; GidA.
DR   InterPro; IPR026904; GidA-assoc_3.
DR   InterPro; IPR002218; GIDA-rel.
DR   InterPro; IPR020595; GIDA-rel_CS.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_assoc_3; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT   CHAIN         1    629       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_0000117105.
FT   NP_BIND      14     19       FAD (By similarity).
FT   NP_BIND     273    287       NAD (Potential).
FT   BINDING     126    126       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     181    181       FAD (By similarity).
FT   BINDING     370    370       FAD (By similarity).
SQ   SEQUENCE   629 AA;  70480 MW;  6D7218C8BEE2239E CRC64;
     MDYHGGTYDV IVVGAGHAGC EAALASARIG AKTLVITLNL DMIAFMPCNP SIGGPAKGIV
     VREIDALGGE MAKNIDKTYI QMRMLNTGKG PAVRALRAQA DKVLYQREMK KTLENQENLT
     LLQGKVERLI VEDGVCKGVI THTGAHYYAK AVVITTGTFL RGEIIIGDIK YSSGPNNQQP
     SIKLSEHLEE LGFELVRFKT GTPPRVNSRT IDYSKTEIQP GDKEPRAFSY ETTKYITDQL
     PCWLTYTTEE THRIIDENLH LSPMYSGMIK GTGPRYCPSI EDKVVRFHDK PRHQIFLEPE
     GRETEEVYVQ GLSTSLPEHI QRKLLETIPG LEKAQLMRAG YAIEYDAIVP TQLWPTLETK
     LVKNLYTAGQ INGTSGYEEA AGQGIMAGIN AAHRALGREE IILSRSDAYI GVLIDDLVTK
     GTNEPYRLLT SRAEYRLLLR HDNADLRLTE LGYRIGLISE ERYQKFLAKK EAIEREKKRL
     QTVIIKPTPK VQEVIREAGG SELKDGIRAA DLLRRPEMTY EHIRKLAPAD EEIAPEVAEQ
     VEIQIKYEGY IQKSLQEVER LKKMENKKIP EDIDYDAIQG LATEARQKLK QVRPLSIAQA
     SRISGVNPAD ISILLVYLEQ GRIARVSNE
//
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