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Database: UniProt
Entry: Q1MPS7
LinkDB: Q1MPS7
Original site: Q1MPS7 
ID   MNMG_LAWIP              Reviewed;         622 AA.
AC   Q1MPS7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   01-OCT-2014, entry version 51.
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=LI0946;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00;
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the
RT   causative agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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; AM180252; CAJ55000.1; -; Genomic_DNA.
DR   RefSeq; YP_595321.1; NC_008011.1.
DR   ProteinModelPortal; Q1MPS7; -.
DR   STRING; 363253.LI0946; -.
DR   GeneID; 4060323; -.
DR   KEGG; lip:LI0946; -.
DR   PATRIC; 22305421; VBILawInt40445_1027.
DR   eggNOG; COG0445; -.
DR   HOGENOM; HOG000201060; -.
DR   KO; K03495; -.
DR   OMA; HTNEQTH; -.
DR   OrthoDB; EOG6W9X6J; -.
DR   BioCyc; LINT363253:GH6E-984-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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD;
KW   Reference proteome; tRNA processing.
FT   CHAIN         1    622       tRNA uridine 5-carboxymethylaminomethyl
FT                                modification enzyme MnmG.
FT                                /FTId=PRO_0000345287.
FT   NP_BIND      11     16       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   NP_BIND     270    284       NAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   BINDING     123    123       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00129}.
FT   BINDING     178    178       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
FT   BINDING     367    367       FAD. {ECO:0000255|HAMAP-Rule:MF_00129}.
SQ   SEQUENCE   622 AA;  68816 MW;  E634512F62666288 CRC64;
     MRTTFDCIVV GGGHAGCEAS MALARLGQKV LLITGNVDRI GHLSCNPAVG GIAKGHIVRE
     IDALGGMMGL WADKAGIQFR TLNRSKGPAV RATRAQVDRD LYMQAVKQDI FSQPNLSVWQ
     DTVEAIIVKD GHTGGVKTAL GQLFNSQYVI LTTGTFLSGL MHIGQKNFSG GRLGDVGTSK
     LSSSLHSIGL HLGRLKTGTT PRLLKTSIDF TSMEMQLGDT PIPSFSFHGP KPSQPQVPCY
     ITWTNEYTHD VIRSGMDRSP MFTGVITGTG ARYCPSIEDK VARFADRDRH QIFVEPEGLT
     SQECYINGIS TSLPLDIQLA LIATIPGLEN AHMVRPGYAI EYDYVDPMQL HPTLETKVLP
     GLWLAGQING TSGYEEAAGQ GLWAALNVFC KITRQEPFIL GRDNAYLAVL VDDLVTQGTK
     EPYRMFTSRA EYRLLLREAN ADIRLTPLGR KIGLVGDYQW NLFQKKISDI DTLVNRLQNI
     RIKPDTLDPS IFLELGESIP NRAYTLEELL KRPSITFQTL RKIYSDLPIT SEDVYLETET
     IIKYAGYLDR QEELVQRSAK LEHSYLPKEI DYTKVAGLSS EVIEKLQIVR PQTLGQAGRI
     SGVTPAAITC LEIYLKKIHA FR
//
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