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Database: UniProt
Entry: B9M9W3
LinkDB: B9M9W3
Original site: B9M9W3 
ID   MNMG_ACIET              Reviewed;         657 AA.
AC   B9M9W3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   14-MAY-2014, entry version 32.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=Dtpsy_0045;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001392; ACM31534.1; -; Genomic_DNA.
DR   RefSeq; YP_002551534.1; NC_011992.1.
DR   ProteinModelPortal; B9M9W3; -.
DR   STRING; 535289.Dtpsy_0045; -.
DR   EnsemblBacteria; ACM31534; ACM31534; Dtpsy_0045.
DR   GeneID; 7382736; -.
DR   KEGG; dia:Dtpsy_0045; -.
DR   PATRIC; 21777062; VBIDiaSp55748_0048.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; NPQIECG; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; AEBR535289:GHOO-45-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    657       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_1000122745.
FT   NP_BIND      13     18       FAD (By similarity).
FT   NP_BIND     281    295       NAD (Potential).
SQ   SEQUENCE   657 AA;  72344 MW;  27D72E86FC3EB0AC CRC64;
     MLYPQDFDVI VVGGGHAGTE AALAAARMGS RTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM ALATDEAGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRR MLENQPNLWL
     FQQAVDDLMV EGDRVVGAVT QVGIRFRSRA VVLTAGTFLD GKIHVGLNNY AAGRAGDPPA
     VSLSARLKEL QLPQGRLKTG TPPRIDGRSI DFSQCEEQPG DGMPGGVNEG AVPVFSFMGN
     AAMHPRQVPC WITHTNARTH EIIRSGFDRS PMFTGKIEGV GPRYCPSVED KINRFADKES
     HQIFLEPEGL TTHEFYPNGI STSLPFDIQY DLVRSMRGLE NAHILRPGYA IEYDYFDPRS
     LKSSFETRQI QGLFFAGQIN GTTGYEEAAA QGLFAGINAA LQCRGERAWV PARDEAYLGV
     LVDDLITKGV TEPYRMFTSR AEFRLQLRED NADMRLTDAG RRMGLVDDAR WDAFSRKRDA
     VSRETERLKS TWVNPRNLPT VEAERVLGKA IEHEYNLFDL LRRPDVGYDA LTTMDGGKYA
     SEAVSRETLG ELSAPVIEQV EIAAKYAGYI ERQRDEVQRA AHFEKLRLPE DLDYMQVAAL
     SIEVRQKLQK HRPETLGQAS RISGVTPAAI SLLMVHLKKG GFKGFAPQPA DGVETVA
//
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