MNMG_LEGPC
ID MNMG_LEGPC Reviewed; 624 AA.
AC A5II62;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=LPC_3175;
OS Legionella pneumophila (strain Corby).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=400673;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Corby;
RA Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT "Identification and characterization of a new conjugation/ type IVA
RT secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT genomic island.";
RL Submitted (NOV-2006) 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}.
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DR EMBL; CP000675; ABQ57062.1; -; Genomic_DNA.
DR RefSeq; WP_011947767.1; NC_009494.2.
DR AlphaFoldDB; A5II62; -.
DR SMR; A5II62; -.
DR KEGG; lpc:LPC_3175; -.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR BioCyc; LPNE400673:LPC_RS15370-MON; -.
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..624
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016618"
FT BINDING 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 624 AA; 69053 MW; CDCAD86A7A1E7688 CRC64;
MNLEQLYDVI VVGGGHAGTE AALAAARLGV KTLLLTHNID LLGQMSCNPA IGGIGKGHLV
KEIDALDGAM AKAADQAGIQ FRILNASKGP AVRATRAQAD RVLYRKAIRT QLQSQANLTI
FQQAVDDLKI EGGLVTGVVT QMGLTLKARA VVLTVGTFLG GKIHVGMNQY AGGRAGDPPS
IALSKSLRDL DLPVGRLKTG TPPRIDRRTI DFSQMVEQPG DTPVPVFSYL GTASDHPQQV
PCHITHTTEA THDIIRNNLD KSPMYAGVIE GVGPRYCPSI EDKIVRFADK TSHQIFVEPE
GLTTEEIYPN GISTSLPFEV QVQFVRTIKG FENAHITRPG YAIEYDYFDP RGLTSFLQTK
AIPNLFFAGQ INGTTGYEEA AAQGIIAGMN AALQIKDQEL WCPRRDEAYI GVLIDDLITC
GTQEPYRMFT SRAEYRLLLR EDNADLRLTE KGRQLGLVGD ERWDSFSKKR EAIESTQALL
HNSWVRVHHN DLFKEALLNP MQHDCRAAEF LKRPEINYQH LLMMDDLNLP ELPQEITEQI
EIQNKYAGYI DRQQQEIEKL RKHENTMLPE TLDYNDVVGL SSEVIQKLNR IKPTSLAQAG
RISGVTPAAL SLLLVHLKKS RLPV