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 01-MAY-2013, entry version 61.
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; AQMSCNP; -.
DR ProtClustDB; PRK05192; -.
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: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
//
