ID MNMG_LISW6 Reviewed; 629 AA.
AC A0AMD1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 01-MAY-2013, entry version 49.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA; OrderedLocusNames=lwe2745;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 /
OS SLCC5334).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / SLCC5334;
RX PubMed=16936040; DOI=10.1128/JB.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R.,
RA Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T.,
RA Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J.,
RA Liang C., Dandekar T., Lampidis R., Kreft J., Goebel W.,
RA Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK22163.1; -; Genomic_DNA.
DR RefSeq; YP_850942.1; NC_008555.1.
DR ProteinModelPortal; A0AMD1; -.
DR STRING; 386043.lwe2745; -.
DR EnsemblBacteria; CAK22163; CAK22163; lwe2745.
DR GeneID; 4465196; -.
DR KEGG; lwe:lwe2745; -.
DR PATRIC; 20332757; VBILisWel39304_2752.
DR eggNOG; COG0445; -.
DR HOGENOM; HOG000201060; -.
DR KO; K03495; -.
DR OMA; AQMSCNP; -.
DR ProtClustDB; PRK05192; -.
DR BioCyc; LWEL386043:GI5X-2764-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 1 629 tRNA uridine 5-carboxymethylaminomethyl
FT modification enzyme MnmG.
FT /FTId=PRO_1000016619.
FT NP_BIND 15 20 FAD (By similarity).
FT NP_BIND 274 288 NAD (Potential).
FT BINDING 127 127 FAD; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 182 182 FAD (By similarity).
FT BINDING 371 371 FAD (By similarity).
SQ SEQUENCE 629 AA; 70122 MW; FAAE26C0400737B6 CRC64;
MQTYDAGTFD VIVVGAGHAG VEAGLASGRM GAKTLMLTIN LDMVAFMPCN PSVGGPAKGV
VVREIDALGG EMGRNTDKTY IQMRMLNTGK GPAVRALRAQ ADKWDYQHEM KHTIEKEENI
TLRQGLVDHL VIEDGVCKGV ITNSGAIYYA KTVVITTGTF SRGEIIVGEL RYSSGPNNQQ
PSVKLSEHLE ELGFELRRFK TGTPPRVKSS TIDYSKTEEQ PGDDHPRAFS FDTVDMMLDQ
LPCWLTYTNE TTHEIIQANL HRSPMFTATK KGTGARYCPS IEDKIVRFSD KPRHQIFLEP
EGKNTEEVYV QGLSTSLPEE VQREMLRTIP GLENVEMMRV GYAIEYDAVM PDQLWPSLET
KLVEGLFTAG QINGTSGYEE AAGQGLMAGI NAARKVFDKE PIILGRDQAY IGVLIDDLVT
KGTEEPYRLL TSRAEYRLLL RHDNADLRLT EIGHEIGLIS DERYERFLAK QSAIEAEKER
LQKTRIKPTA EVQAMLKEIG SGELKDGILA ADLLRRPEIT YDKIAQIVSR ETFITDEIAE
QVEIQVKYEG YIQKSNLQVE KMKRMEDKKI PENIDYDAIS GLATEALEKL KKIEPLSIAQ
ASRISGVNPA DISILLVYIE QGKIAKISK
//
