ID A0A0G1DD24_9BACT Unreviewed; 610 AA.
AC A0A0G1DD24;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=UV38_C0001G0277 {ECO:0000313|EMBL:KKS68736.1};
OS candidate division TM6 bacterium GW2011_GWE2_42_60.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619076 {ECO:0000313|EMBL:KKS68736.1, ECO:0000313|Proteomes:UP000034453};
RN [1] {ECO:0000313|EMBL:KKS68736.1, ECO:0000313|Proteomes:UP000034453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS68736.1}.
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DR EMBL; LCEG01000001; KKS68736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1DD24; -.
DR STRING; 1619076.UV38_C0001G0277; -.
DR PATRIC; fig|1619076.3.peg.292; -.
DR Proteomes; UP000034453; 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 PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 528..599
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 610 AA; 67608 MW; B55FE8A93BE218EF CRC64;
MHVLEKTPLF FDTIVIGGGH AGVEAAAAAA RMGVSTALIT LRADRIGFMP CNPSIGGIGK
GHIVFEISAL GGLMPKLCTQ SYLQAKMLNT SKGPAVQGLR LQIDKHLYAQ CAQKALASIP
HLSIIEAMVD ELLCSEQKRI EGVRLADGRI LHCSTVIVTG GTFLNGIVHI GEESYPAGRS
DEPSIINLAA SMKQLGIRMG RMKTGTPARL LRSSVDVSCM ERDIAEPLDY LYEFHPHHAV
TKEECFITHT NAETHRIILE SAQRSPIFSK RITGTPTRYC PAIEDKLVRF SHKDAHHVFV
EPEGLDSEEL YPNGISNSLP KDIQERFIQS IKGFEKAVIT RYAYGIEYDF VHPEQLSHTL
ELKTCPGLFF AGQINGTTGY EEAAGQGLIA GINAALAVKK EPPYSMSRNE GYIGIMIDDL
VSMGVDEPYR MFTSRAERRL ILRQDNVFAR LSGKAFALGL ISNELFTEID AEINKVQATL
DFMQAQDKYK TFAQLISNNY PERVKQEIKR LSPHALSPRA LETVYAEILY APYKKRELKE
VEKNEAYRAL SIPSDLVYQG MPGLSHELKE KLIRLAPKTI AQAALIQGMT PATISLLIFR
VREHTAQKRS
//
