ID MNMG_COXBU Reviewed; 627 AA.
AC P94613;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 27-MAR-2024, entry version 130.
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=CBU_1924;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile phase I;
RA Willems H., Jaeger C.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; Y10436; CAA71459.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO91415.2; -; Genomic_DNA.
DR RefSeq; NP_820901.2; NC_002971.3.
DR RefSeq; WP_010958541.1; NZ_CCYB01000002.1.
DR AlphaFoldDB; P94613; -.
DR SMR; P94613; -.
DR STRING; 227377.CBU_1924; -.
DR DNASU; 1209837; -.
DR EnsemblBacteria; AAO91415; AAO91415; CBU_1924.
DR GeneID; 1209837; -.
DR KEGG; cbu:CBU_1924; -.
DR PATRIC; fig|227377.7.peg.1906; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..627
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117091"
FT BINDING 14..19
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"
FT CONFLICT 12
FT /note="V -> A (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> Y (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="R -> H (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="Q -> R (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="L -> I (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="V -> L (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="F -> V (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..330
FT /note="IK -> KT (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="E -> A (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="A -> T (in Ref. 1; CAA71459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 69969 MW; 6354640D5DB4837E CRC64;
MQSTSQQFDV IVVGGGHAGT EAALVAARMG ARTLLLTHNI ETLGQMSCNP AIGGIGKSHL
VKEIDALGGI MALAADQAGI HFRTLNARKG PAVRATRAQA DRVLYKAAIH HALENQPHLW
LFQQGVDDLI IQNNRAAGVV TQMGLAFYAP TVILTVGTFL GGKIHIGMNH YRGGRAGDPP
ALALAERLRE MPFRVERLKT GTPPRIDGRT INYSQLIEQP SDQPLPLMSY WSHGEDRPRQ
VSCFITQTNE KTHDIIRNGL KTSPLFSGVI EGVGPRYCPS IEDKIVRFAD RNSHQLFLEP
EGLNTPEVYP NGVSTSLSFD VQLDFIHSIK GLEKCHITRP GYAIEYDYFD PRDLKPSLET
KYVPGLYFAG QINGTTGYEE AAAQGLIAGI NAALQIQERA PWTPARDEAY IGVLIDDLTT
RGTNEPYRMF TSRAEYRLLL RQDNADLRLT EKGRDLGCVD DERWNFFVKK KETIEKEQQR
LKKQRIWPKS TVAKAIESRF QQLLERDYSA MDLLRRPEIN YPALMQIEEL GPAVLEPSVA
EQIDIQAKYE GYLTHQLAEI ARQKKYQTAQ IPSSLDYNQV TGLSNEVRQK LNETKPTTLG
QASRIPGITP AAISLLLVHL KKKELYP
//
