ID A0A7V1DK03_9BACT Unreviewed; 459 AA. AC A0A7V1DK03; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 6. 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 Name=mnmG {ECO:0000313|EMBL:HEA84271.1}; GN ORFNames=ENI03_03205 {ECO:0000313|EMBL:HEA84271.1}; OS Thermodesulfobacterium geofontis. OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales; OC Thermodesulfobacteriaceae; Thermodesulfobacterium. OX NCBI_TaxID=1295609 {ECO:0000313|EMBL:HEA84271.1}; RN [1] {ECO:0000313|EMBL:HEA84271.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HyVt-36 {ECO:0000313|EMBL:HEA84271.1}; RX PubMed=31911466; RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.; RT "Genome- and Community-Level Interaction Insights into Carbon Utilization RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal RT Sediment."; RL mSystems 5:e00795-e00719(2020). 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:HEA84271.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DRHB01000137; HEA84271.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7V1DK03; -. 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; -; 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; IPR026904; MnmG_C. DR InterPro; IPR040131; MnmG_N. 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR TIGRFAMs; TIGR00136; gidA; 1. DR PROSITE; PS01280; GIDA_1; 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 8..399 FT /note="GIDA" FT /evidence="ECO:0000259|Pfam:PF01134" FT DOMAIN 402..459 FT /note="GIDA_C" FT /evidence="ECO:0000259|Pfam:PF13932" FT NON_TER 459 FT /evidence="ECO:0000313|EMBL:HEA84271.1" SQ SEQUENCE 459 AA; 51201 MW; C902E55BD4CE8C28 CRC64; MRFLESFDVI VIGAGHAGIE ASLAASRMGC KTLLITINLE RIGAMSCNPS IGGIGKGHLV KEIDALGGEM ALAIDETGIQ FRKLNTKKGP AVRATRAQAD RFRYQERMKR TLERVPNLFI KQSLVTRLLI KDKRVIGIET KAGEEFEAKA VVIAPGTFLH GLIHIGLESF PAGRMGDPPS NRLPEHLREL GFEMGRFKTG TCPRIDGRTI DYSKLEIQWG DFPPPLFSFK NKGKRPPLPQ VPCFITYTTE KTHEIIRNAL DRSPLFTGKI KGRGVRYCPS IEDKVFRFPD KERHQVFLEP EGLDTVEVYP NGISTSLPID VQWEMVRSIP GLEKAEILRP GYGIEHDYVI PTQLKHTLET KFISGLFLAG QINGTTGYEE AAAQGLIAGI NAALYVKEEQ PLILDRSQAY IGVLIDDLVT KGTDEPYRMF TSRAEYRLLL REDNADLRLT EIGKKIGLV //