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Database: UniProt
Entry: A0AMD1
LinkDB: A0AMD1
Original site: A0AMD1 
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   29-OCT-2014, entry version 57.
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=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. {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; 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; FHIEREQ; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; LWEL386043:GI5X-2828-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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    629       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_1000016619.
FT   NP_BIND      15     20       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   NP_BIND     274    288       NAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   BINDING     127    127       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00129}.
FT   BINDING     182    182       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   BINDING     371    371       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
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
//
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