ID A0A2T6D862_9BACT Unreviewed; 626 AA.
AC A0A2T6D862;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=DB354_05010 {ECO:0000313|EMBL:PTX98625.1};
OS Opitutus sp. ER46.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=2161864 {ECO:0000313|EMBL:PTX98625.1, ECO:0000313|Proteomes:UP000244023};
RN [1] {ECO:0000313|EMBL:PTX98625.1, ECO:0000313|Proteomes:UP000244023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER46 {ECO:0000313|EMBL:PTX98625.1,
RC ECO:0000313|Proteomes:UP000244023};
RA Buenger W., Mueller J., Hurek T., Reinhold-Hurek B.;
RT "Genomic and phenotypic characterization of four novel plant-associated
RT Verrucomicrobia indicate a new subdivision with one cultivated member.";
RL Submitted (MAR-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PTX98625.1}.
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DR EMBL; QAYX01000018; PTX98625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6D862; -.
DR InParanoid; A0A2T6D862; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000244023; 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 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; 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 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:UP000244023};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 541..612
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 292..306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 626 AA; 69301 MW; 36861BFA04738AFB CRC64;
MNTSDTCFDV IVCGAGHAGV EAALAAARMD ASTLLVTGNI DTIAQMSCNP AIGGQAKGQI
VREIDALGGE MAINTDVTGI QFRLLNESKG PAVQSPRAQC DKKAYQFRLK HTLELHPRLQ
LFQATVTGLI YDYGKVVGCR TNLDVEFRGR SVVVTTGTFL RGLMHIGKNK NEGGRLGDFS
AKTLSQSFLD AGIELQRLKT GTPPRLLGRS LDFSRMQEQR GDAEPTFFAF HDTRDDGELF
HVEQTGERRL GWRPGCEQVS CWMTYTTAET AQLVRDNLHL SAMYSGEIEG VGPRYCPSIE
DKFVRFADKP RHLLFLEPEG RTTDEFYVNG LSTSLPFEVQ VRMIHSVPGL ENAVLLRPAY
AVEYDFAPPT QLFPTLESRK VENLFFAGQI NGTSGYEEAA CQGLVAGVNA VNKVRGLPPL
LIGRHEGYIG VLIDDLVTKG TQEPYRMFTS RAEHRLLFNH GSAELRLAHH AKVHGLISAT
RLARIEDKRR RIERWVSRLE VGRTHAGTYA EGLRRNGAPS ELPAEFLKES VGVKEEVLYR
VRYQGYLARE HRQIEKLASI EAVRIPPDID YAQVRGLRKE STLKLGQLRP MTLGQASRVS
GVNPADIGVL MVWIAARQGR GAAPSE
//