ID F9P2G6_STRMT Unreviewed; 637 AA.
AC F9P2G6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=HMPREF9178_1389 {ECO:0000313|EMBL:EGR93855.1};
OS Streptococcus mitis bv. 2 str. F0392.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=768726 {ECO:0000313|EMBL:EGR93855.1, ECO:0000313|Proteomes:UP000003771};
RN [1] {ECO:0000313|EMBL:EGR93855.1, ECO:0000313|Proteomes:UP000003771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0392 {ECO:0000313|EMBL:EGR93855.1,
RC ECO:0000313|Proteomes:UP000003771};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (JUL-2011) 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: 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:EGR93855.1}.
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DR EMBL; AFUO01000001; EGR93855.1; -; Genomic_DNA.
DR RefSeq; WP_000221895.1; NZ_AFUO01000001.1.
DR AlphaFoldDB; F9P2G6; -.
DR PATRIC; fig|768726.4.peg.1303; -.
DR eggNOG; COG0445; Bacteria.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000003771; 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 tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00129}.
FT DOMAIN 549..620
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 276..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
FT BINDING 373
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 637 AA; 71047 MW; E4E85155907A3777 CRC64;
MTYNFTEEYD IIVIGAGHAG VEASLAASRM GCKVLLATIN IEMLAFMPCN PSIGGSAKGI
VVREVDALGG EMAKNIDKTY IQMKMLNTGK GPAVRALRAQ ADKELYSKEM RKTVENQENL
TLRQTMIDEI LVEDGKVVGV RTATHQEYGA KAVIVTTGTA LRGEIIIGDL KYSSGPNHSL
ASINLADNLK ELGLEIGRFK TGTPPRVKAS SINYDVTEIQ PGDEAPNHFS YTSRDEDYVK
DQVPCWLTYT NGTSHEIIQN NLHRAPMFTG VVKGVGPRYC PSIEDKIVRF ADKERHQLFL
EPEGRNTEEV YVQGLSTSLP EDVQRELVHS IKGLENAEMM RTGYAIEYDM VLPHQLRATL
ETKKISGLFT AGQTNGTSGY EEAAGQGIIA GINAALKIQG KPELILKRSD GYIGVMIDDL
VTKGTIEPYR LLTSRAEYRL ILRHDNADMR LTEMGREIGL VDDERWARFE IKKNQFDNEM
KRLDIIKLKP VKETNAKVEE MGFKPLTDAV TAKEFLRRPE VSYQDVVAFI GPAAEDLDDK
IIELIETEIK YEGYISKAMD QVAKMKRMEE KRIPANIDWD DIDSIATEAR QKFKLINPET
IGQASRISGV NPADISILMV YLEGKNRSIS KNQEKKA
//
