ID A0A3S0J3X1_9BACI Unreviewed; 631 AA.
AC A0A3S0J3X1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ECO:0000313|EMBL:RTQ93760.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=EKG35_07435 {ECO:0000313|EMBL:RTQ93760.1};
OS Lysinibacillus telephonicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1714840 {ECO:0000313|EMBL:RTQ93760.1, ECO:0000313|Proteomes:UP000276349};
RN [1] {ECO:0000313|EMBL:RTQ93760.1, ECO:0000313|Proteomes:UP000276349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5H2222 {ECO:0000313|EMBL:RTQ93760.1,
RC ECO:0000313|Proteomes:UP000276349};
RA Yu L.;
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RTQ93760.1}.
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DR EMBL; RXNR01000016; RTQ93760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0J3X1; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000276349; Unassembled WGS sequence.
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; 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:UP000276349};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 547..618
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 16..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 183
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 275..289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 631 AA; 70428 MW; 5267A34B8669DE71 CRC64;
MTTTYEAGQY DVIVIGAGHA GVESAYAAAK MGAKTLMVTI NLDMIAFMPC NPSVGGPAKG
IVVREIDALG GVMGKVIDKT HIQMRMLNTG KGPAVRALRA QADKVLYQRE MKRLLEEEEN
LTIHQSIVDE LIIEDDTVRG VITQTGAIYR AKAVIITTGT YLRGEIIIGE LKYSSGPNNQ
QPSIKLADNL RDLGFEMVRF KTGTPPRVDS KTIDYSKTEI QPGDDVPRAF SFETTEFIMD
QIPCWLTYTS PETHQIINDN LDKAPMYTGA ITGTGPRYCP SIETKIVRFN DKPRHQLFLE
PEGRDTQEVY VQGLSTSLPE HIQRQMLQTI PGLEKAEMMR AGYAIEYDSI VPTQLWPTLE
TKRIKNLYTA GQINGTSGYE EAAGQGLMAG INAAAKVLGK EEVILKRSEA YIGVLIDDLV
TKGTNEPYRL LTSRAEYRLL LRHDNADLRL TELGYKLGLI SEERFAKFTE KKEQIENEIA
RLREVIIKPN ETTQAVIRSV GGAELKDGIR AADLVKRTEM TYDLVASLSP AEYEFSEEVK
EQIEVQLKYE GYIQKALQQV EKLHKMENKK IPEDIDYDEI SSLATEAREK LKEVRPLSIA
QASRISGVNP ADISILLVYI EQGKIARISN E
//
