ID   T0YSG2_9ZZZZ            Unreviewed;       276 AA.
AC   T0YSG2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme GidA {ECO:0000313|EMBL:EQD34772.1};
GN   ORFNames=B1A_18558 {ECO:0000313|EMBL:EQD34772.1};
OS   mine drainage metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD34772.1};
RN   [1] {ECO:0000313|EMBL:EQD34772.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mendez C., Richter M., Ferrer M., Sanchez J.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EQD34772.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA   Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA   Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA   Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA   Ferrer M.;
RT   "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT   along an acid mine drainage.";
RL   ISME J. 8:1259-1274(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EQD34772.1}.
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; AUZX01013698; EQD34772.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0YSG2; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR049312; GIDA_C_N.
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   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   SMART; SM01228; GIDA_assoc_3; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          191..262
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
SQ   SEQUENCE   276 AA;  30556 MW;  7E99B2980EA3C1FC CRC64;
     MYFAGQINGT TGYEEAAAQG LLAGINATLA LREAEPWIPG RSDGYLGVLV DDLVTRGTRE
     PYRMFTSRAE HRLLLREDNA DARLTPVGRT LGLVDDERWR FFEAKRRRID GEVERLRALR
     IHPADLEAQW SARVLGASLA RDVSAFELLR RPEVAYGTLL EIAAPHAGDA SAEEADERIA
     AQLSVQVEAL AKYAGYIERQ LEEVARQRRN EETRLPEDID YAQIAGLSHE VRVRLNEYRP
     ATLGQAGRVP GVTPAALSLL LVHLKKRAPG AGSRVA
//