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-MAY-2013, entry version 45.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG;
DE AltName: Full=Glucose-inhibited division protein A;
GN Name=mnmG; Synonyms=gidA; 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 (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; 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; AQMSCNP; -.
DR ProtClustDB; PRK05192; -.
DR BioCyc; LINT363253:GH6E-1102-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; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; FAD; Flavoprotein; NAD; tRNA processing.
FT CHAIN 1 622 tRNA uridine 5-carboxymethylaminomethyl
FT modification enzyme MnmG.
FT /FTId=PRO_0000345287.
FT NP_BIND 11 16 FAD (By similarity).
FT NP_BIND 270 284 NAD (Potential).
FT BINDING 123 123 FAD; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 178 178 FAD (By similarity).
FT BINDING 367 367 FAD (By similarity).
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
//
