ID A0A124FKZ4_9BACT Unreviewed; 447 AA.
AC A0A124FKZ4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG {ECO:0000256|ARBA:ARBA00020461};
DE AltName: Full=Glucose-inhibited division protein A {ECO:0000256|ARBA:ARBA00031800};
DE Flags: Fragment;
GN ORFNames=XD68_1659 {ECO:0000313|EMBL:KUK38784.1};
OS Synergistales bacterium 54_24.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK38784.1, ECO:0000313|Proteomes:UP000054050};
RN [1] {ECO:0000313|Proteomes:UP000054050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000256|ARBA:ARBA00025948}.
CC -!- SIMILARITY: Belongs to the MnmG family.
CC {ECO:0000256|ARBA:ARBA00007653}.
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:KUK38784.1}.
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DR EMBL; LGFQ01000128; KUK38784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FKZ4; -.
DR STRING; 1635272.XD68_1659; -.
DR PATRIC; fig|1635272.3.peg.666; -.
DR Proteomes; UP000054050; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004416; MnmG.
DR InterPro; IPR002218; MnmG-rel.
DR InterPro; IPR020595; MnmG-rel_CS.
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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01281; GIDA_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 6..395
FT /note="MnmG N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01134"
FT NON_TER 447
FT /evidence="ECO:0000313|EMBL:KUK38784.1"
SQ SEQUENCE 447 AA; 48698 MW; 80BC0B8171D2E70F CRC64;
MDKIYDVIVV GGGHAGCEAA LAASRMGASV LLLNLHLENT ALMACNPSIG GPAKGHITRE
IDALGGEQGK ATDAAALHMR VLNTSKGPAV RALRAQCDMR SYYEYFLERL ESAKNVDIHQ
AVVEDIWVEG KCVRGVKTNL GVVFEGRKVI LATGTYLGGR VHIGLVNFPS GPLGEVPAGG
LASSLKKLGF EVGTLKTGTS PRIHADSVDF GSLMRQEGDA VPRAFSYFDE GKVYSGFPCY
VTRSTLKTHE IIKRALDRSP LFTGAIKGVG PRYCPSIEDR VVRFPEKDSH IVFLEPTARR
SREIYMQNFS TSLPYDVQVA MVRSLPGCEG AHLLRPGYAI EYNFLPPTQL RPWLETKLVE
GLFCAGQING TSGYEEAASQ GLLAGINAVL TLRGEEPLVL KRSEAYIGVL VDDLVTKGTS
EPYRMLTSRC EHRLLLRFDN ADRRLSP
//
