ID   MNMG_BORBZ              Reviewed;         621 AA.
AC   B7J1B1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=BbuZS7_0178;
OS   Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=445985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS7;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
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; CP001205; ACK74835.1; -; Genomic_DNA.
DR   RefSeq; WP_002657592.1; NC_011728.1.
DR   AlphaFoldDB; B7J1B1; -.
DR   SMR; B7J1B1; -.
DR   PRIDE; B7J1B1; -.
DR   EnsemblBacteria; ACK74835; ACK74835; BbuZS7_0178.
DR   GeneID; 56567605; -.
DR   KEGG; bbz:BbuZS7_0178; -.
DR   HOGENOM; CLU_007831_2_2_12; -.
DR   OMA; FRPGYAI; -.
DR   OrthoDB; 146811at2; -.
DR   Proteomes; UP000006901; 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; tRNA processing.
FT   CHAIN           1..621
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme MnmG"
FT                   /id="PRO_1000117715"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT   BINDING         270..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ   SEQUENCE   621 AA;  70130 MW;  4BFA4F195AF01E5D CRC64;
     MDFDAIVIGG GHAGIEAALA LSRLNFKTLM ITQNLDTIGK LSCNPAIGGL AKGNMVREID
     ALGGEMGRII DFSMIQFRVL NKSRGPAVQA PRAQADKLMY QTKAKETLER QDNLDLFQDT
     VVDFLLNSMR NEIEGVVTER GNKFRSSVVV LTTGTFLRGK IFIGEYRADM GRLAEFSAYG
     LDKTLLGLGF EMGRLKTGTP ARIHKKSVDF SKTEVQFGDS DIIPFSFSNG KLDKSQLSCY
     VTYTNKKTHE IISENMHLSP LYSGEIVGNG PRYCPSIEDK IVKFKDKDRH QIFIEPEGFN
     TEEMYLNGLS SSLPENIQQK LINSIEGLEH AVITRPGYAV EYDYINPIEL YPNLESKRVK
     GLFIAGQTNG SSGYEEAAAQ GLMAGINAAL RLQNKKPMIL TRTSSYIGVL IDDLVTKGTK
     EPYRMFTSRA EHRLNLRHDT SDKRLIKIGY DLGLVDEKRY SRYLFKESRV EEIKELLKQR
     RLSLKDVVDE QLKKHVSKDF YHILKDPSIS LDNLIKIDPS LSDSKVILEQ VELDVKYEGY
     INRQKDLIKR LDNLELVKLP FDFNYEIIEG LSREAREKFS KIQPATLAQA SRIPGIRSTD
     ITVLLIYFSN PKNKVVINFS L