ID A0A0D7PBI4_9BRAD Unreviewed; 627 AA.
AC A0A0D7PBI4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=UP09_10200 {ECO:0000313|EMBL:KJC47522.1};
OS Bradyrhizobium sp. LTSP885.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1619232 {ECO:0000313|EMBL:KJC47522.1, ECO:0000313|Proteomes:UP000032343};
RN [1] {ECO:0000313|Proteomes:UP000032343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LTSP885 {ECO:0000313|Proteomes:UP000032343};
RX PubMed=25909973; DOI=10.1038/ismej.2015.54;
RA VanInsberghe D.S., Maas K.R., Cardenas E., Strachan C.R., Hallam S.J.,
RA Mohn W.;
RT "Non-symbiotic Bradyrhizobium ecotypes dominate North American forest
RT soils.";
RL ISME J. 9:2435-2441(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}.
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:KJC47522.1}.
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DR EMBL; JYMT01000015; KJC47522.1; -; Genomic_DNA.
DR RefSeq; WP_044538009.1; NZ_JYMT01000015.1.
DR AlphaFoldDB; A0A0D7PBI4; -.
DR STRING; 1619232.UP09_10200; -.
DR PATRIC; fig|1619232.5.peg.838; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000032343; Unassembled WGS sequence.
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:UP000032343};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 542..612
FT /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT enzyme C-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01228"
FT BINDING 14..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 273..287
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 627 AA; 67232 MW; 2A4A50F23E69C54C CRC64;
MTSPAGSFDV IVIGGGHAGC EAAAAAARMG AETALVTHRF STIGAMSCNP AIGGLGKGHL
VREVDALDGL MGRVADAGGI QFRMLNRRKG PAVRGPRAQA DRKLYAAAMQ AAISETANLS
VIEGEADELI VTDGRVTGVR LGNGRIVCAG AVVITTGTFL RGLIHLGEKN WPAGRVGEAP
AMGLSTSFER ADFILGRLKT GTPPRLDGST IDWSAVEMQP GDDPPEPFSV MTDRITTPQI
QCGITRTTPA THEVIRANVH RSPMYSGQIK SSGPRYCPSI EDKIVRFGDR DGHQIFLEPE
GLDDTTVYPN GISTSLPEEV QLAILASIPG LERVRMVRPG YAIEYDHVDP RELDPTLQTK
RLRGLFLAGQ INGTTGYEEA AGQGIVAGLN AALTASGADP IVFDRADGYL GVMIDDLVTR
GITEPYRMFT SRAEYRLTLR ADNADQRLTD KGIALGCVGA ARTERHRTKM AALEAAKTLA
KSLSITPNEA TKHGLSLNRD GHRRSAFELL AYPEIEWPAV QAIWPELSAI DPAIAVHLEI
DAKYDVYLKR QTADVDAFRR DEGLVLTDVD YADVPGLSNE ARAKLEKAQP RTVGQAGRID
GMTPAALGIL AAYLRREARR KTAKVTA
//
