MNMG_BORAP
ID MNMG_BORAP Reviewed; 621 AA.
AC Q0SNY6; G0IR22;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BAPKO_0180, BafPKo_0175;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(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}.
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DR EMBL; CP000395; ABH01442.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69408.1; -; Genomic_DNA.
DR RefSeq; WP_011600872.1; NC_017238.1.
DR AlphaFoldDB; Q0SNY6; -.
DR SMR; Q0SNY6; -.
DR STRING; 390236.BafPKo_0175; -.
DR EnsemblBacteria; AEL69408; AEL69408; BafPKo_0175.
DR KEGG; baf:BAPKO_0180; -.
DR KEGG; bafz:BafPKo_0175; -.
DR PATRIC; fig|390236.22.peg.173; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_12; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000005216; 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_1000016555"
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; 70167 MW; 9B75AC62E61752BA CRC64;
MDFDAIVIGG GHAGIEAALA ISRLNFKTLM ITQNLDTIGK LSCNPAIGGL AKGNMVREID
ALGGEMGRII DFSMIQFRVL NKSRGPAVQA PRAQADKLMY QTKAKETLER QDNLDLFQDT
VVDFLLNSMR NEIEGVVTER GNKFRSSVVV LTTGTFLRGK IFIGEYRANM GRLAEFSAYG
LDKTLLGLGF EMGRLKTGTP ARIHRKSVDF SKTEVQFGDS DIIPFSFSNG KLDKSQLSCY
VTYTNKRTHE IISENMHLSP LYSGEIVGNG PRYCPSIEDK IVKFKDKDRH QIFIEPEGFN
TEEMYLNGLS SSLPENVQQK LINSIEGLEH AVITRPGYAV EYDYINPIEL YPSLESKRVK
GLFIAGQTNG SSGYEEAAAQ GLMAGINAAL RLQNKKPMIL TRTSSYIGVL IDDLVTKGTK
EPYRMFTSRA EHRLNLRHDT SDKRLIKIGY DLGLVDEERY SKYLFKKRRV EEIKELLKQR
RLSLKDIADE QLKKHVNKDF YHILKDPSIS LDNLIKIDPS LSDSKVILEQ VELDIKYEGY
INRQKDLIKK LHNLELVKLP FDFNYGIIEG LSREAREKFS KVQPATLAQA SRIPGIRNTD
ITVLFIYFSN PKNKVVLNFS V