ID A0A0A8JGG5_BACSX Unreviewed; 629 AA.
AC A0A0A8JGG5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=OXB_0965 {ECO:0000313|EMBL:BAQ09437.1};
OS Bacillus sp. (strain OxB-1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ09437.1, ECO:0000313|Proteomes:UP000031651};
RN [1] {ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAQ09437.1, ECO:0000313|Proteomes:UP000031651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OxB-1 {ECO:0000313|EMBL:BAQ09437.1,
RC ECO:0000313|Proteomes:UP000031651};
RA Yamaguchi T., Asano Y.;
RT "Complete Genome Sequence of an Aldoxime Degrader, Bacillus sp. OxB-1.";
RL Genome Announc. 3:e00025-15(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, 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}.
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DR EMBL; AP013294; BAQ09437.1; -; Genomic_DNA.
DR RefSeq; WP_041072389.1; NZ_AP013294.1.
DR AlphaFoldDB; A0A0A8JGG5; -.
DR STRING; 98228.OXB_0965; -.
DR KEGG; baco:OXB_0965; -.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000031651; Chromosome.
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 Gene3D; 1.10.10.1800; tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG/GidA; 1.
DR HAMAP; MF_00129; MnmG_GidA; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR049312; GIDA_C_N.
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 Pfam; PF21680; GIDA_C_1st; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM01228; GIDA_assoc_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS01280; GIDA_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000031651};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 546..617
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 15..20
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 629 AA; 70088 MW; 1E48938C9DA666A9 CRC64;
MPKFEAGTFD CIVIGAGHAG AEAALSAAKM GASTLVLTMN LDMIAFMPCN PSLGGPAKGI
VVREIDALGG AMGKVIDKTH IQMRMLNTGK GPAVRALRAQ ADKVLYQQEM KRIMESQENL
TLRQGVVEEL IVEEDEVKGV ITQIGAIYRA KTVIITTGTF LRGEIIIGDL KYSSGPNNQM
PSISLADNIR ELGFEMVRFK TGTPPRINSK TIDYSKTEIQ PGDDVPRAFS YETTEFIMDQ
LPCWLTYTSP TTHQIINENL HLSPMYSGMI KGKGPSYCPS IEDKIVRFAD KSRHQIFLEP
EGRNTNEIYV QGLSTSLPEH VQRRLIESVP GLEKAEMMRA GYAIEYDSVV ATQLWPTLET
KRIRNLYTAG QINGTSGYEE AAAQGLMAGI NAACRVLGKE ERVLARSDAY IGVLIDDLVT
KGTSEPYRLL TSRAEYRLLL RHDNADMRLT EIGYELGLIS EERHKKFLVK KQQIEEEIER
LRKISIKPNE EIQEIIRAAG GTELRESIKA ADLLKRPEMK YNDIIRITPS EEQLSEEVAE
QVEIFIKYEG YIQKSMQQVE RLKKMENKKI PENIDYDAIS GIAKEAKANL NQVRPLSIAQ
ASRISGVNPA DISILLVYIE QGKIAKISG
//
