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Database: UniProt
Entry: A4XN50
LinkDB: A4XN50
Original site: A4XN50 
ID   MNMG_CALS8              Reviewed;         626 AA.
AC   A4XN50;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   14-MAY-2014, entry version 46.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE   AltName: Full=Glucose-inhibited division protein A;
GN   Name=mnmG; Synonyms=gidA; OrderedLocusNames=Csac_2770;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L.,
RA   Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M.,
RA   Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W.,
RA   Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) 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; CP000679; ABP68335.1; -; Genomic_DNA.
DR   RefSeq; YP_001181526.1; NC_009437.1.
DR   ProteinModelPortal; A4XN50; -.
DR   STRING; 351627.Csac_2770; -.
DR   EnsemblBacteria; ABP68335; ABP68335; Csac_2770.
DR   GeneID; 5087495; -.
DR   KEGG; csc:Csac_2770; -.
DR   PATRIC; 21255432; VBICalSac56748_2998.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; HTNEQTH; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; CSAC351627:GJ17-2835-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    626       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_1000016573.
FT   NP_BIND      14     19       FAD (By similarity).
FT   NP_BIND     273    287       NAD (Potential).
SQ   SEQUENCE   626 AA;  69893 MW;  DAFAEF6E9828A11E CRC64;
     MEFVAGEYDI VVVGAGHAGC EAALACARLG LKTIVFAINL DSIGNMPCNP SIGGTGKGHL
     VREIDALGGE MGKAADATAI QVRILNRAKG PAVYSLRAQC DRARYKLYMK RVLESQPNLD
     IRQGEVCDIL VEDGKVTGVK LTTGAIFRAK AVVLATGTFL GGRIIIGETV YDGGPDGMHP
     AKYLTESLKK LGIEMMRFKT GTPARVHRRS LDFSKMQIQL GDEVITPFSF EHETLEIEQV
     PCYLTYTTEE THRIIRENLH RAPLFTGLIQ GVGPRYCPSI EDKVVRFADK PRHQVFIEPM
     GRDTEEMYVQ GMSSSLPEDV QIKMYRSVIG LENVQIMRPA YAIEYDCINP LQLEATLQFK
     KIKGLFSAGQ INGTSGYEEA AAQGIIAGIN AAMYVKGKEM LVLDRSQAYI GVLIDDLVTK
     GTNEPYRIMT SRAEYRLILR QDNADLRLTE IGYRIGLISQ ERYEKFLKKK KMIEDEIERL
     KKTVIAPSDK VNKFLIEHGS SPISTGVKLS ELLKRPELSY EALREIDPQR PDLPRSVKEE
     VEIEIKYEGY IKKQLQQIEQ FKKLENKKIP EWVDYNQISG LSTEAKQKLS QIRPASIGQA
     SRISGVSPAD ISVLLIWLEQ AKKGSK
//
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