MNMG_RHOBA
ID MNMG_RHOBA Reviewed; 653 AA.
AC Q7ULV7;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 98.
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}; OrderedLocusNames=RB9255;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD76162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294149; CAD76162.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_868785.1; NC_005027.1.
DR AlphaFoldDB; Q7ULV7; -.
DR SMR; Q7ULV7; -.
DR STRING; 243090.RB9255; -.
DR PRIDE; Q7ULV7; -.
DR EnsemblBacteria; CAD76162; CAD76162; RB9255.
DR KEGG; rba:RB9255; -.
DR PATRIC; fig|243090.15.peg.4432; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_0; -.
DR InParanoid; Q7ULV7; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000001025; 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; 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; Reference proteome; tRNA processing.
FT CHAIN 1..653
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000117162"
FT REGION 624..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..23
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 287..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 653 AA; 71391 MW; 6415CDB109D4DF44 CRC64;
MTANNPQNRY DYDVVVIGAG HAGTEAAAAA ARLGAKTALL TTNLDTVGQM SCNPAIGGVA
KGQIVREVDA LGGLMGEAID ATGIQFRMLN RRKGPAMHSP RAQADKKAYQ NFIKYRIETQ
DNLDLRQETV EDLITEPIAD GQDRLANQRV IGVRVRGDAV YHAPTVILTT GTFLQAIMHT
GKSQSAGGRA GEGTTAGLSG ALKGMGFTLD RFKTGTPPRL NARTIDYSGL EEQPGDDDPQ
PFSYLNDAIS SPQMACHIAH TNERVHDLIR ANLDRAPMYS GQIDSRGPRY CPSIEDKVVR
FADKSSHQLF LEPEGRQTCE VYVNGISTSL PRDVQDAMFR CIPGLEKAAI MRYGYAVEYD
YCPPTQLWPH LESKSVSGLF FAGQINGTTG YEEAAGQGLI AGLNAARTAA SKTPWVPSRQ
DAYIGVLVDD LVTSGTDEPY RMFTSRAEYR LLLRQDNADR RLTAQADELG LIDAARRERF
HRKLAEIERG TELLQQAKFQ PETGPTVRGD VYLRRPEVTW NVIAEQVPEL AGIGREAAEQ
CSIDIKYAGY IDRQQAEVHK QSRHAEKSIP VSFDYDKIGP LRNEAKEKLT KVRPLNLGQA
KRISGITPAD LALVLAHLEN NSLSQTKSSA SVDKRASSDN ESSRPTSSAS DSL
