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MNMG_LEPCP
ID   MNMG_LEPCP              Reviewed;         685 AA.
AC   B1XYL1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Lcho_4196;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-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) of
CC       certain tRNAs, forming tRNA-cmnm(5)s(2)U34. {ECO:0000255|HAMAP-
CC       Rule:MF_00129}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00129};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC       {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; CP001013; ACB36447.1; -; Genomic_DNA.
DR   RefSeq; WP_012349188.1; NC_010524.1.
DR   AlphaFoldDB; B1XYL1; -.
DR   SMR; B1XYL1; -.
DR   STRING; 395495.Lcho_4196; -.
DR   EnsemblBacteria; ACB36447; ACB36447; Lcho_4196.
DR   KEGG; lch:Lcho_4196; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_4; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000001693; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 1.10.150.570; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR044920; MnmG_C_subdom.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT   CHAIN           1..685
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_0000345292"
FT   BINDING         13..18
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         284..298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   685 AA;  74573 MW;  900E7B77DB4F7AD5 CRC64;
     MLYPQEFDVI VVGGGHAGTE AALAAARMGC DTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
     KEVDALGGAM AAATDESGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRQ RLENQPHLWL
     FQQAVDDLMV EGDRVVGAVT QVGIRFRART VVLTAGTFLD GKIHVGLNNY PAGRAGDPPA
     VSLSARLKEL KLPQGRLKTG TPPRIDGRSI DFSKLIEQPG DGVAAADGTP ASSPMPVFSF
     LGSAAQHPRQ MPCWITNTNQ RTHDILRTGF DRSPMFTGVI EGVGPRYCPS IEDKINRFAD
     KNSHQIFLEP EGLTTNEYYP NGISTSLPFD IQLAAVRTML GMENAYILRP GYAIEYDYFD
     PRELKTSFES KAIGGLFFAG QINGTTGYEE AAAQGLYAGA NAALQAQGNP PLSFGRDQAY
     LGVLVDDLIT KGVTEPYRMF TSRAEFRLQL REDNADMRLT EIGRSVGLVD DVRWDAFNRK
     RDAVSRETER LKSTWVHPAI LPAADSERLF GKALEHEYNL ADLMRRPGIS YDTVAEALTI
     ARPGNYVSRE TLNSQLGADL AAAVIEQLEI AIKYAGYIDK QNEDVQRAAH YEHLRLPDEL
     DYAQVTALSF EVRQKLTKHR PETLGQASRI SGVTPAALSL LLIHLKRGRF KGFTGNDKVA
     AGPISADAVN TDINDNPAHA ATDAA
 
 
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