ID A0A172Q9S7_9STRE Unreviewed; 632 AA.
AC A0A172Q9S7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461, ECO:0000256|HAMAP-Rule:MF_00129};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800, ECO:0000256|HAMAP-Rule:MF_00129};
GN Name=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=A0O21_09515 {ECO:0000313|EMBL:AND80216.1};
OS Streptococcus pantholopis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1811193 {ECO:0000313|EMBL:AND80216.1, ECO:0000313|Proteomes:UP000077317};
RN [1] {ECO:0000313|EMBL:AND80216.1, ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|EMBL:AND80216.1,
RC ECO:0000313|Proteomes:UP000077317};
RX PubMed=27226124; DOI=10.1099/ijsem.0.001189;
RA Bai X., Xiong Y., Lu S., Jin D., Lai X., Yang J., Niu L., Hu S., Meng X.,
RA Pu J., Ye C., Xu J.;
RT "Streptococcuspantholopis sp. nov., isolated from faeces of the Tibetan
RT antelope (Pantholops hodgsonii).";
RL Int. J. Syst. Evol. Microbiol. 66:3281-3286(2016).
RN [2] {ECO:0000313|Proteomes:UP000077317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA 26 {ECO:0000313|Proteomes:UP000077317};
RA Bai X.;
RT "Streptococcus antelopensis sp. nov., isolated from the feces of the
RT Tibetan antelope (Pantholops hodgsonii) in Hoh Xil National Nature Reserve,
RT Qinghai, China.";
RL Submitted (MAR-2016) 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.
CC {ECO:0000256|ARBA:ARBA00003717, ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00129};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|ARBA:ARBA00025948, ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129}.
CC -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000256|ARBA:ARBA00007653,
CC ECO:0000256|HAMAP-Rule:MF_00129}.
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DR EMBL; CP014699; AND80216.1; -; Genomic_DNA.
DR RefSeq; WP_067064627.1; NZ_CP014699.1.
DR AlphaFoldDB; A0A172Q9S7; -.
DR STRING; 1811193.A0O21_09515; -.
DR KEGG; spat:A0O21_09515; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000077317; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.150.570; GidA associated domain, C-terminal subdomain; 1.
DR Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
DR InterPro; IPR026904; MnmG_C.
DR InterPro; IPR047001; MnmG_C_subdom.
DR InterPro; IPR044920; MnmG_C_subdom_sf.
DR InterPro; IPR040131; MnmG_N.
DR NCBIfam; TIGR00136; gidA; 1.
DR PANTHER; PTHR11806; GLUCOSE INHIBITED DIVISION PROTEIN A; 1.
DR PANTHER; PTHR11806:SF0; PROTEIN MTO1 HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF01134; GIDA; 1.
DR Pfam; PF13932; GIDA_C; 1.
DR Pfam; PF21680; GIDA_C_1st; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00129};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00129};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00129};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00129};
KW Reference proteome {ECO:0000313|Proteomes:UP000077317};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 549..620
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 15..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 276..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 373
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 632 AA; 70055 MW; D8EA7329A8D384D6 CRC64;
MTQEFVEDYD VIVIGAGHAG VEAALASSRM GCKTLLATIN LEMLAFMPCN PSIGGSAKGI
VVREIDALGG EMGKNIDKTY IQMRMLNTGK GPAVRALRAQ ADKALYARTM KHTVEQQENL
TLRQTMIEEI LVEDGKVLGV RTATNQKFSA ESVIVTTGTA LRGEIILGDL KYSSGPNNSL
PSIGLADNLR ELGLEIGRFK TGTPPRVKAS SIDYAETEIQ PGDKKANHFS FLSDDADYLQ
EQIPCWLTYT NPKSHDIIHK NLHRAPMFSG IVKGVGPRYC PSIEDKIVRF ADKERHQLFL
EPEGRETEEV YVQGLSTSLP EDVQKELLHS IKGLEKAELM RTGYAIEYDV VLPHQLRATL
ETKLVSGLFT AGQTNGTSGY EEAAGQGLIA GINAALKVQG QPEFILKRSD AYIGVMIDDL
VTKGTAEPYR LLTSRAEYRL ILRHDNADMR LTELGRKIGL VDDERYYVYK RRKEQFDKEL
TRLSSSKLKP VTETNERIAE LGFKPLTDAL TAKDFMRRPG INYDLVTSFI GAADESLDDN
VIELLETEIK YEGYINKALD QVAKMKRLEG KPIPKNIDWD AIDSIATEAR QKFKKINPET
IGQASRISGV NPSDISILMV YLEGKQKAGS KS
//
