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Database: UniProt
Entry: Q7W2I1
LinkDB: Q7W2I1
Original site: Q7W2I1 
ID   MNMG_BORPA              Reviewed;         639 AA.
AC   Q7W2I1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-SEP-2014, entry version 68.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=BPP0001;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640423; CAE39742.1; -; Genomic_DNA.
DR   RefSeq; NP_882367.1; NC_002928.3.
DR   RefSeq; WP_010927257.1; NC_002928.3.
DR   ProteinModelPortal; Q7W2I1; -.
DR   SMR; Q7W2I1; 1-561.
DR   STRING; 257311.BPP0001; -.
DR   EnsemblBacteria; CAE39742; CAE39742; BPP0001.
DR   GeneID; 1666999; -.
DR   KEGG; bpa:BPP0001; -.
DR   PATRIC; 21143537; VBIBorPar43418_0001.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; HTNEQTH; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; BPAR257311:BPP0001-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    639       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_0000117064.
FT   NP_BIND      13     18       FAD (By similarity).
FT   NP_BIND     274    288       NAD (Potential).
SQ   SEQUENCE   639 AA;  70151 MW;  F0C452ADE5740043 CRC64;
     MDFPREFDVI VVGGGHAGTE AALAAARAGA QTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AIATDEAGIQ FRILNSSKGP AVRATRVQAD RVLYRNAMRA RLENQPNLWL
     FQQAVDDLMV QGDQVVGAVT QIGLRFRART VVLTAGTFLN GLIHVGLQNY SGGRAGDPPA
     NSLGQRLKEL QLPQGRLKTG TPPRIDGRSI NYSVLEEQPG DLDPVPVFSF LGKASMHPRQ
     LPCWITHTNA RTHEIIRGGL DRSPMYSGVI EGVGPRYCPS IEDKIHRFAD KASHQVFLEP
     EGLNTHEIYP NGVSTSLPFD VQYELIHSLP GLENAHILRP GYAIEYDYFD PRALKSTLET
     KAISGLFFAG QINGTTGYEE AAAQGLLAGA NAALQAQGKE PWVPRRDEAY LGVLVDDLVT
     RGVTEPYRMF TSRAEYRLSL REDNADLRLT EIGRRLGLVD DVRWDAFSRK RDAVAQEVER
     LKSTWVNPRV LPAHAAEALL GKAIEREYSL SDLLKRPNVS YEALMQARTD EGELLAGPGV
     LEDDVLAEQV ETQVKYAGYI ARQQDEVQKH LSHEQQPIPA DIDYDAVTSL SFEVRQKLKT
     HRPETIGQAA RVSGVTPAAI SLLLIHLKRL HYGSRKQAA
//
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