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Database: UniProt
Entry: A6QKK1
LinkDB: A6QKK1
Original site: A6QKK1 
ID   MNMG_STAAE              Reviewed;         625 AA.
AC   A6QKK1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   19-FEB-2014, entry version 48.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=NWMN_2611;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/JB.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and
RT   comparative analysis of staphylococcal genomes: polymorphism and
RT   evolution of two major pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
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; AP009351; BAF68883.1; -; Genomic_DNA.
DR   RefSeq; YP_001333645.1; NC_009641.1.
DR   ProteinModelPortal; A6QKK1; -.
DR   SMR; A6QKK1; 4-620.
DR   STRING; 426430.NWMN_2611; -.
DR   EnsemblBacteria; BAF68883; BAF68883; NWMN_2611.
DR   GeneID; 5331950; -.
DR   KEGG; sae:NWMN_2611; -.
DR   PATRIC; 19589104; VBIStaAur133992_2827.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201060; -.
DR   KO; K03495; -.
DR   OMA; YINGLST; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   ProtClustDB; PRK05192; -.
DR   BioCyc; SAUR426430:GIXC-2684-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    625       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_1000071417.
FT   NP_BIND      11     16       FAD (By similarity).
FT   NP_BIND     270    284       NAD (Potential).
FT   BINDING     123    123       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     178    178       FAD (By similarity).
FT   BINDING     367    367       FAD (By similarity).
SQ   SEQUENCE   625 AA;  70116 MW;  27CA7DD9B0C99BD9 CRC64;
     MVQEYDVIVI GAGHAGVEAG LASARRGAKT LMLTINLDNI AFMPCNPSVG GPAKGIVVRE
     IDALGGQMAK TIDKTHIQMR MLNTGKGPAV RALRAQADKV LYQQEMKRVI EDEENLHIMQ
     GMVDELIIED NEVKGVRTNI GTEYLSKAVI ITTGTFLRGE IILGNMKYSS GPNHQLPSIT
     LSDNLRELGF DIVRFKTGTP PRVNSKTIDY SKTEIQPGDD VGRAFSFETT EYILDQLPCW
     LTYTNAETHK VIDDNLHLSA MYSGMIKGTG PRYCPSIEDK FVRFNDKPRH QLFLEPEGRN
     TNEVYVQGLS TSLPEHVQRQ MLETIPGLEK ADMMRAGYAI EYDAIVPTQL WPTLETKMIK
     NLYTAGQING TSGYEEAAGQ GLMAGINAAG KVLNTGEKIL SRSDAYIGVL IDDLVTKGTN
     EPYRLLTSRA EYRLLLRHDN ADLRLTDMGY ELGMISEERY ARFNEKRQQI DAEIKRLSDI
     RIKPNEHTQA IIEQHGGSRL KDGILAIDLL RRPEMTYDII LELLEEEHQL NADVEEQVEI
     QTKYEGYINK SLQQVEKVKR MEEKKIPEDL DYSKIDSLAT EAREKLSEVK PLNIAQASRI
     SGVNPADISI LLIYLEQGKL QRVSD
//
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