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