MNMG_BORBU
ID MNMG_BORBU Reviewed; 621 AA.
AC P53362;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
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}; OrderedLocusNames=BB_0178;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RX PubMed=1490605; DOI=10.1016/0378-1097(92)90034-l;
RA Old I.G., Macdougall J.H., Saint-Girons I., Davidson B.E.;
RT "Mapping of genes on the linear chromosome of the bacterium Borrelia
RT burgdorferi: possible locations for its origin of replication.";
RL FEMS Microbiol. Lett. 78:245-250(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 597-621.
RC STRAIN=212;
RA Old I.G.;
RL Submitted (FEB-1996) 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}.
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; Z12160; CAA78149.1; -; Genomic_DNA.
DR EMBL; AJ003222; CAA06005.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66557.2; -; Genomic_DNA.
DR EMBL; X95669; CAA64972.1; -; Genomic_DNA.
DR EMBL; X95668; CAA64968.1; -; Genomic_DNA.
DR PIR; B70122; B70122.
DR RefSeq; NP_212312.2; NC_001318.1.
DR RefSeq; WP_002657592.1; NC_001318.1.
DR AlphaFoldDB; P53362; -.
DR SMR; P53362; -.
DR STRING; 224326.BB_0178; -.
DR PRIDE; P53362; -.
DR EnsemblBacteria; AAC66557; AAC66557; BB_0178.
DR GeneID; 56567605; -.
DR KEGG; bbu:BB_0178; -.
DR PATRIC; fig|224326.49.peg.575; -.
DR HOGENOM; CLU_007831_2_2_12; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000001807; 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..621
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117066"
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
