ID   MNMG_PEDPA              Reviewed;         637 AA.
AC   Q03D60;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=PEPE_1843;
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000422; ABJ68862.1; -; Genomic_DNA.
DR   RefSeq; WP_011673924.1; NC_008525.1.
DR   AlphaFoldDB; Q03D60; -.
DR   SMR; Q03D60; -.
DR   STRING; 278197.PEPE_1843; -.
DR   PRIDE; Q03D60; -.
DR   EnsemblBacteria; ABJ68862; ABJ68862; PEPE_1843.
DR   GeneID; 33062041; -.
DR   KEGG; ppe:PEPE_1843; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_9; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000000773; 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.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; NAD; Reference proteome; tRNA processing.
FT   CHAIN           1..637
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000016635"
FT   BINDING         18..23
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         282..296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   637 AA;  71105 MW;  B4CD03F5EF1B7917 CRC64;
     MSEVKQYEGR EYDVIVVGAG HAGSEAALAA ARMGNKTLLM TINLDMVAFM PCNPSIGGPA
     KGIVVREIDA LGGEMGRNID KTYVQMRMLN TGKGPAVRAL RAQADKHAYH AEMKKTIEAE
     PNLTLRQGIV DDLIVEDGVC KGVITNTGAR YQAKSVVLTL GTAARGKIII GELQYSSGPN
     NSQAALELTK NLTEKYHFDL ERFKTGTPPR VDGGTINYDE TEEQPGDEVP NHFSFQTPDS
     KYIELKNQLS CWLTYTNEKT HEIIRENLDR APMFSGMIEG VGPRYCPSIE DKIVRFADKS
     RHQLFLEPEG RKTDEWYVQG LSTSMPEEVQ QQILHSIKGL EEAEMMRPGY AIEYDVVAPY
     QLKNTLETKL VKNLYTAGQT NGTSGYEEAA GQGLIAGINA GRRALGKEPL TLKRSDAYIG
     VMIDDLVTKG TKEPYRLLTS RAEYRLILRH DNADLRLTEV GHNLGLVSDE EYNAFLEKKQ
     DIKDELQRLS EIRIKPSQVQ KFLESKGSNG LKDGVLASEF LRRPEVNYSD LLKFIDAPEK
     DLDRRVIEQV EIETKYAGYI KKAQDRVDRL KRMEEKAIPD RIDYEAINGL ATEGRQKLEK
     IRPTTIAQAS RISGVTPADI AILSVYIQQG KIAKIAE