ID A0A0D6EYF1_9PROT Unreviewed; 637 AA.
AC A0A0D6EYF1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=gidA {ECO:0000256|HAMAP-Rule:MF_00129,
GN ECO:0000313|EMBL:CEZ20283.1};
GN Synonyms=mnmG {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=BN1208_1403 {ECO:0000313|EMBL:CEZ20283.1};
OS Candidatus Methylopumilus planktonicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ20283.1, ECO:0000313|Proteomes:UP000064007};
RN [1] {ECO:0000313|Proteomes:UP000064007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000064007};
RA Salcher M.M.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LN827929; CEZ20283.1; -; Genomic_DNA.
DR RefSeq; WP_046489118.1; NZ_LN827929.1.
DR AlphaFoldDB; A0A0D6EYF1; -.
DR STRING; 1581557.BN1208_1403; -.
DR KEGG; mbat:BN1208_1403; -.
DR HOGENOM; CLU_007831_2_2_4; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000064007; Chromosome 1.
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 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:UP000064007};
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 13..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 180
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"
FT BINDING 370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 637 AA; 70901 MW; E2A3AFA58A3B18BF CRC64;
MEFPNNFDVI VVGGGHAGTE AALASARMGQ KTLLLTHNIE TLGQMSCNPS IGGIGKGHLV
KEIDALGGAM GIATDEAGIQ FRILNSSKGP AVRATRAQAD RILYKAAIRH RLENQPNLWL
FQQAVDDILL EKDHVAGVVT QIGIQFKSRT VVLTAGTFLG GLVHVGLKNY QAGRAGDPPS
MSLAHRLREI GLPVGRLKTG TPPRIDGRTI NYAVMQEQPG DNPTPYLSFY GKKTTHPRQV
SCWITHTNES THDIIRSGLD RSPMYTGVIE GVGPRYCPSV EDKIHRFADK DSHQIFLEPE
GLDTNEIYPN GISTSLPFDI QYKLVRSING LENAHILRPG YAIEYDYFDP RNLKSSLETK
SIQGLFFAGQ INGTTGYEEA AAQGLLAGTN AALMTQDKDA WCPKRDEAYL GVLVDDLITR
GVTEPYRMFT SRAEYRLMLR EDNADLRLTS MGRNLGLVDD ERWTMFNKKQ ETIHSEEARL
KKFFIRPQDI SIEKQEAIIG KAIDHEYSLF DLLRRPEVSF AGVKELMKED ADLIDPAVRE
QVEISAKYKG YIVRQQEEVD RSRDQLDFPL PLDLDYKDVH GLSAEAQQKL NLHKPENLGQ
ASRISGITPA TISLLLVFIK RKNKPKKMTA KRPAKAA
//
