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Database: UniProt
Entry: W4V8T8_9FIRM
LinkDB: W4V8T8_9FIRM
Original site: W4V8T8_9FIRM 
ID   W4V8T8_9FIRM            Unreviewed;       154 AA.
AC   W4V8T8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=tRNA uridine 5-carboxymethylaminomethyl modification enzyme GidA {ECO:0000313|EMBL:GAE89243.1};
GN   ORFNames=JCM21531_2749 {ECO:0000313|EMBL:GAE89243.1};
OS   Acetivibrio straminisolvens JCM 21531.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=1294263 {ECO:0000313|EMBL:GAE89243.1, ECO:0000313|Proteomes:UP000019109};
RN   [1] {ECO:0000313|EMBL:GAE89243.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21531 {ECO:0000313|EMBL:GAE89243.1};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Clostridium straminisolvens Strain JCM 21531T,
RT   Isolated from a Cellulose-Degrading Bacterial Community.";
RL   Genome Announc. 2:e00110-14(2014).
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   -!- 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:GAE89243.1}.
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DR   EMBL; BAVR01000033; GAE89243.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4V8T8; -.
DR   STRING; 1294263.JCM21531_2749; -.
DR   Proteomes; UP000019109; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR002218; MnmG-rel.
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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019109};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          9..154
FT                   /note="MnmG N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01134"
SQ   SEQUENCE   154 AA;  16511 MW;  B1EAA69D8CC8900A CRC64;
     MGFVAGEYDV AVVGAGHAGC EAALACARLG VKTVVFAINL DSIANMPCNP NIGGTAKGHL
     VREIDALGGE MGKNTDKTFI QSKILNSAKG PAVFSLRAQV DRRSYQIEMK NTLEQQENLD
     VKQAEIVEIL YDEIEGKKAV TGVKTIQGRY IKAK
//
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