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Database: UniProt
Entry: B1KQ45
LinkDB: B1KQ45
Original site: B1KQ45 
ID   MNMG_SHEWM              Reviewed;         630 AA.
AC   B1KQ45;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   01-OCT-2014, entry version 41.
DE   RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000255|HAMAP-Rule:MF_00129};
DE   AltName: Full=Glucose-inhibited division protein A {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Name=mnmG {ECO:0000255|HAMAP-Rule:MF_00129};
GN   Synonyms=gidA {ECO:0000255|HAMAP-Rule:MF_00129};
GN   OrderedLocusNames=Swoo_4909;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) 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. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
CC   -!- COFACTOR: FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00129}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
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DR   EMBL; CP000961; ACA89158.1; -; Genomic_DNA.
DR   RefSeq; YP_001763253.1; NC_010506.1.
DR   ProteinModelPortal; B1KQ45; -.
DR   SMR; B1KQ45; 1-552.
DR   STRING; 392500.Swoo_4909; -.
DR   EnsemblBacteria; ACA89158; ACA89158; Swoo_4909.
DR   GeneID; 6119290; -.
DR   KEGG; swd:Swoo_4909; -.
DR   PATRIC; 23612603; VBISheWoo126588_5056.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201059; -.
DR   KO; K03495; -.
DR   OMA; HTNEQTH; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; SWOO392500:GI2C-5074-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:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
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   PRINTS; PR00368; FADPNR.
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;
KW   Reference proteome; tRNA processing.
FT   CHAIN         1    630       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_0000345332.
FT   NP_BIND      13     18       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   NP_BIND     273    287       NAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   BINDING     125    125       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00129}.
FT   BINDING     180    180       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   BINDING     370    370       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
SQ   SEQUENCE   630 AA;  69639 MW;  E8D9F95D9339154A CRC64;
     MHFHERFDVI VIGGGHAGTE AALAAARMGS KTLLLTHNID TLGQMSCNPA IGGIGKGHLV
     KEIDALGGAM AIATDYAGIQ FRTLNSSKGP AVRATRAQAD RALYRAKIQE ILQNQPNLRL
     FQQAVDDLIV ENGRVTGVVT QMGLAFEAPA VVLTAGTFLS GKIHIGMQNY SGGRAGDPPS
     IALADRLREL PIRIGRLKTG TPPRIDANTI NFDLMTEQKG DTPLPVMSFI GDVSQHPKQI
     SCFVTHTNEK THDIIRGGLD RSPMYSGVIE GVGPRYCPSI EDKIHRFADK SSHQIFIEPE
     GLNTNEIYPN GISTSLPFDV QLNLVRSIKG MENAEIIRPG YAIEYDYFDP RDLKNSLETK
     SIDGLFFAGQ INGTTGYEEA GAQGLLAGMN ASLQVQGKEI WCPRRDEAYL GVLVDDLSTL
     GTKEPYRMFT SRAEYRLLLR EDNADLRLTE KGREIGLVDD ERWAKFSEKR ESIELELQRL
     RSQWVHPNSP LIDVLNPELN TPISREASFE DLLRRPEMDY PKLMSLEGFG PGLDDPRAAE
     QVQIQVKYSG YIQRQQDEID KAIRHETTGL PLDLDYQEVP GLSNEVIAKL NDHKPETIGQ
     ASRISGMTPA AISILLVHLK RRGLLRKKAS
//
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