ID A0A2S9GSG0_9BURK Unreviewed; 645 AA.
AC A0A2S9GSG0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=S2091_4643 {ECO:0000313|EMBL:PRC90635.1};
OS Solimicrobium silvestre.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Solimicrobium.
OX NCBI_TaxID=2099400 {ECO:0000313|EMBL:PRC90635.1, ECO:0000313|Proteomes:UP000237839};
RN [1] {ECO:0000313|EMBL:PRC90635.1, ECO:0000313|Proteomes:UP000237839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S20-91 {ECO:0000313|EMBL:PRC90635.1,
RC ECO:0000313|Proteomes:UP000237839};
RA Margesin R., Albuquerque L., Zhang D.-C., Froufe H.J.C., Severino R.,
RA Roxo I., Egas C., Da Costa M.S.;
RT "Solimicrobium silvestre gen. nov., sp. nov., isolated from alpine forest
RT soil.";
RL Submitted (FEB-2018) 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}.
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:PRC90635.1}.
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DR EMBL; PUGF01000041; PRC90635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9GSG0; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000237839; 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 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:UP000237839};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 553..624
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 274..288
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 645 AA; 71041 MW; 4D048737A1CE273D CRC64;
MFYPKEFDVI IVGGGHAGTE AALASARMGQ STLLLTHNIE TLGQMSCNPS IGGIGKGHLV
KEVDAMGGAM AIATDEAGIQ FRILNSSKGP AVRATRAQAD RILYKQAIRS RLENQPNLYL
FQQAVDDLLI EGDRVVGAVT QVGIKFKARA VVLTAGTFLD GKIHVGLSQY AAGRAGDPPA
ISLSSRLKEL SLPQGRLKTG TPPRIDGRSI DFSVMQEQPG DLDPVPVFSV LGNAKMHPRQ
VPCWITHTNQ QTHDIIRTGL DRSPMYTGVI EGVGPRYCPS IEDKIHRFSG KESHQIFLEP
EGLTTNEFYP NGISTSLPFD IQLALVRSMN GMENAYILRP GYAIEYDYFD PRGLKASLET
RQIQGLFFAG QINGTTGYEE AAAQGMLAGL NAALFTQQKD AWVPGRSEAY LGVLVDDLIT
KGVQEPYRMF TSRAEFRLSL REDNADMRLT EIGRKLGCVS DLQWAAFEIK RESVARELER
LKSTWVNPRL IADAEAERVV GKALEREYSL VDLLRRPQVS YESLMTLRGV DGQDVAGPAV
QDAAVKEQVE IHVKYEGYID RQAKEVQKHA HFENLPMPDN FDYLDVSGLS IEVKQKLNQQ
KPETLGQCSR ISGVTPAAIS LLLVHLKKRG FKEFSQTPTL VEGSI
//
