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 01-MAY-2013, entry version 63.
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 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; AQMSCNP; -.
DR ProtClustDB; PRK05192; -.
DR BioCyc; BPAR257311:BPP0001-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 1 639 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
//
