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-MAY-2013, entry version 35.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA; 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 (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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; AQMSCNP; -.
DR ProtClustDB; PRK05192; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA: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; tRNA processing.
FT CHAIN 1 630 tRNA uridine 5-carboxymethylaminomethyl
FT modification enzyme MnmG.
FT /FTId=PRO_0000345332.
FT NP_BIND 13 18 FAD (By similarity).
FT NP_BIND 273 287 NAD (Potential).
FT BINDING 125 125 FAD; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 180 180 FAD (By similarity).
FT BINDING 370 370 FAD (By similarity).
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
//
