MNMG_PSEA7
ID MNMG_PSEA7 Reviewed; 631 AA.
AC A6VF43;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=PSPA7_6367;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) 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; CP000744; ABR82051.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VF43; -.
DR SMR; A6VF43; -.
DR EnsemblBacteria; ABR82051; ABR82051; PSPA7_6367.
DR KEGG; pap:PSPA7_6367; -.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR Proteomes; UP000001582; 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..631
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000016643"
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"
SQ SEQUENCE 631 AA; 69706 MW; BCB726C06AF88AB5 CRC64;
MVDFPTRFDV IVIGGGHAGT EAALAAARMG VKTLLLTHNV ETLGQMSCNP AIGGIGKSHL
VKEIDALGGA MAEATDKGGI QFRILNSRKG PAVRATRAQA DRVLYKAAIR HTLENQPNLW
IFQQACDDLI VEQDQVRGVV TQMGLRFHAD NVVLTTGTFL GGLIHIGLEN YSGGRAGDPP
SIALARRLRE LPLRVGRLKT GTPPRIDGRS VVFSVMTEQP GDTPIPVMSF LGSKEQHPEQ
VSCWITHTNA RTHEIIAANL DRSPMYSGVI EGIGPRYCPS IEDKIHRFAD KESHQVFLEP
EGLTTHELYP NGISTSLPFD VQLQIVRSIR GMENAHIVRP GYAIEYDFFD PRDLKYSLET
KVIGGLFFAG QINGTTGYEE AGAQGLLAGA NAALRAQGKD SWCPRRDEAY IGVLVDDLIT
LGTQEPYRMF TSRAEYRLIL REDNADLRLT EKGRELGLVD DRRWAAFEAK REGIEREEQR
LKSTWVRPNT PQGEAIAERF GTPLTHEYNL LNLLSRPEID YASLVEITGD AVDNPQVAEQ
VEIRTKYAGY IDRQQEEIAR LRASEDTRLP VDIDYLGISG LSKEIQNKLN QARPETLGQA
SRIPGVTPAA ISLLLIHLKK RASGRQLEQS A
