MNMG_THISH
ID MNMG_THISH Reviewed; 639 AA.
AC B8GRC9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=Tgr7_3316;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL74383.1; -; Genomic_DNA.
DR RefSeq; WP_012639845.1; NC_011901.1.
DR AlphaFoldDB; B8GRC9; -.
DR SMR; B8GRC9; -.
DR STRING; 396588.Tgr7_3316; -.
DR PRIDE; B8GRC9; -.
DR EnsemblBacteria; ACL74383; ACL74383; Tgr7_3316.
DR KEGG; tgr:Tgr7_3316; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_6; -.
DR OMA; FRPGYAI; -.
DR OrthoDB; 146811at2; -.
DR Proteomes; UP000002383; 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; Reference proteome; tRNA processing.
FT CHAIN 1..639
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme MnmG"
FT /id="PRO_1000122757"
FT REGION 620..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 639 AA; 69544 MW; 1B6FB2E060A62EC6 CRC64;
MGFEASYDVI VVGGGHAGTE AALASARAGA RTLLLTHNIE TIGQMSCNPA IGGIGKGHLV
KEIDALGGLM ARAADRGGIH FRTLNSRKGP AVRATRAQAD RVRYKAAVRS VVENTPHLFL
FQQAVDDLIV EGERVAGVIT QTGLRFRSPA VVLTVGTFLG GRIHVGEVQH AGGRAGDPPS
IALAARLREL APRVGRLKTG TPPRIDGRSI DYAQLTEQPG DAPRPVFSFI GARDEHPPQV
SCWIARTTEH THAIIRGALH RSPMYSGAIE GVGPRYCPSI EDKVVRFADK DSHQVFIEPE
GLDTHEVYPN GISTSLPFDV QFELVRSIPG FEQAHITRPG YAIEYDYFDP RDLKPSLETR
CLAGLFFAGQ INGTTGYEEA AAQGLVAGLN AARSVRDLAP WCPRRDEAYI GVLIDDLITR
GTAEPYRMFT SRAEYRLMLR EDNADLRLTP LGRDMGLVDD ARWAAFCTKR EAVERETQRL
AATRLDPERV DREAAERVIG GAFSREQNLL DLLRRPEVDY AALMGLEGAG PGVEDPRVAE
QVEIGAKYAG YIQRQQDEVA RQQRHENLAL PEGLDYAAIT GLSMEVRQKL AAHRPHTLGQ
AARIPGVTPA AVSLLLVHVK RQGGNGPQSP RPDDGRARA
