MNMG_BURCJ
ID MNMG_BURCJ Reviewed; 656 AA.
AC B4E581;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-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=BceJ2315_00240; ORFNames=BCAL0024;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR50330.1; -; Genomic_DNA.
DR RefSeq; WP_006482726.1; NC_011000.1.
DR AlphaFoldDB; B4E581; -.
DR SMR; B4E581; -.
DR STRING; 216591.BCAL0024; -.
DR EnsemblBacteria; CAR50330; CAR50330; BCAL0024.
DR KEGG; bcj:BCAL0024; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR BioCyc; BCEN216591:G1G1V-26-MON; -.
DR Proteomes; UP000001035; Chromosome 1.
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..656
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000095644"
FT REGION 637..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 274..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 656 AA; 71906 MW; 10E0473602ACC6CF CRC64;
MLFPTEFDVI VVGGGHAGTE AALASARMGA KTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
KEVDALGGAM AAATDESGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRH RLENQPNLWL
FQQAVDDLMV EGDRVVGAVT QIGIRFRARA VVLTAGTFLD GKIHVGLNNY TGGRAGDPAA
VSLSSRLKEL KLPQGRLKTG TPPRIDGRTI DFSKLDEQPG DLDPIPVFSF LGRAEQHPQQ
LPCWVTHTNE RTHDIIRGGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFAS KESHQIFLEP
EGLTTNEFYP NGISTSLPFD VQLELVHSMR GLENAHILRP GYAIEYDYFD PRALKASLET
KAINGLFFAG QINGTTGYEE AAAQGLLAGL NAGRYVQEKE AWCPRRDQAY LGVLVDDLVT
RGVAEPYRMF TSRAEYRLSL REDNADMRLT EIGRELGLVD DARWDAFSRK RDAVSRETER
LKSTWVTPKT LPAEEATALL GKAIDHEYSL AELLRRPGVS YDGVCGLKGG ECGPAEPLTD
DPVLLEQIKE QVEIGIKYQG YIERQASEIE RNDANENTRL PDGIDYREVR GLSFEVSQKL
NEFRPETIGQ ASRISGVTPA AISLLMVHLK RRGLGRRNGT AAEAAEQGGG TVPTQQ