MNMG_CHLL3
ID MNMG_CHLL3 Reviewed; 621 AA.
AC Q3B6Y3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=Plut_0006;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB22898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000096; ABB22898.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041463950.1; NC_007512.1.
DR AlphaFoldDB; Q3B6Y3; -.
DR SMR; Q3B6Y3; -.
DR STRING; 319225.Plut_0006; -.
DR EnsemblBacteria; ABB22898; ABB22898; Plut_0006.
DR KEGG; plt:Plut_0006; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_10; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000002709; 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..621
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_0000345313"
FT REGION 199..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
FT BINDING 269..283
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00129"
SQ SEQUENCE 621 AA; 68106 MW; AF7890C1763B4108 CRC64;
MYDVIVAGAG HAGTEAALAV SRSGLSCLLV TTDLNAVARM SCNPAIGGVA KGQITREIDA
LGGEMAKAID STGIQFRMLN LSKGPAMHSP RAQADRVAYT AYMKRALEEE VNLDLLQDTV
TGIEQREGIL RGVRLLSGRL VTGRAAILTC GTFLNGLIHI GMDHYPGGRT IAEPPVTGLT
ENLILAGFEA GRLKTGTPPR IDRRSVDYSR VEEQKGDENP PPFSFSTPTL KGRAQLSCYV
THSSERTHEI LKTGFDRSPL FTGKVQGIGP RYCPSIEDKI FRFPDRPGHH IFLEPEGFET
NEMYVNGFST SLPEDIQIDG LRSMKGLEEV KLIRAGYAIE YDYFPPYQIH STLETKRIRN
LYFAGQINGT SGYEEAAAQG LLAGINAAAD ILKRPALRLK RSDAYIGVLV DDLVTKEMKE
PYRMFTSSAE HRLMLRHDNA DIRLMHFGHQ SGLVSDAAME RCRTKMRAIG EIKALTEKTA
IPAEVLDSLI SKQGQPHAAS GQKISAAIKR PGMSLEILMN SLPPFREALL SISTDKEAHQ
QVEIDLKYEG YLKRELLTAD KIARLDALQI PSEYNYSCIK GLSSEGVEKL ISHRPETLGQ
ASRISGVSPS DISVLMVHIG R