ID T1ZHA1_STRIT Unreviewed; 638 AA.
AC T1ZHA1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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 ECO:0000313|EMBL:AGU77205.1};
GN Synonyms=gidA {ECO:0000256|HAMAP-Rule:MF_00129};
GN ORFNames=SIR_1874 {ECO:0000313|EMBL:AGU77205.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU77205.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU77205.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU77205.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003857; AGU77205.1; -; Genomic_DNA.
DR RefSeq; WP_021003357.1; NZ_UZBH01000005.1.
DR AlphaFoldDB; T1ZHA1; -.
DR KEGG; sib:SIR_1874; -.
DR PATRIC; fig|862967.3.peg.1899; -.
DR eggNOG; COG0445; Bacteria.
DR HOGENOM; CLU_007831_2_2_9; -.
DR OrthoDB; 9815560at2; -.
DR Proteomes; UP000016233; 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:UP000016233};
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 276..290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00129"
SQ SEQUENCE 638 AA; 71529 MW; 2D6991B0AF49AFF8 CRC64;
MTHNFTESYD IVVIGAGHAG VEASLAASRM GCKVLLATIN IEMLAFMPCN PSIGGSAKGI
VVREVDALGG EMAKNIDKTY IQMKMLNTGK GPAVRALRAQ ADKELYSREM RKTVQHQENL
TLRQTVIDEI LVENGKVIGV KTATHQEFAA KAVVVTTGTA LRGEIIIGDL KYSSGPNHSL
AAISLADNLR DLGFEIGRFK TGTPPRIKAS SINYEETDIQ PGDEKANHFS YISRDEDYLK
DQIPCWLTYT NEMSHEIIQN NLYRAPMFSG MVKGVGPRYC PSIEDKIVRF ADKERHQLFL
EPEGRDTEEV YIQGLSTSLP EDVQKDLVHS IKGLENAELM RTGYAIEYDM IMPHQLRATL
ETKKISGLFT AGQTNGTSGY EEAAGQGIVA GINAALKVQE KPELILKRSD GYIGVMIDDL
VTKGTVEPYR LLTSRAEYRL ILRHDNADMR LTEIGRKVGL VDDERWLRFE IKKHQYETEM
KRLNSIKLKP IKETNEMVEK LGFKPLTDAV TAKEFLRRPE VSYEDVINFI GPAAEVLDEK
IIELIETEVK YEGYISKALD QVEKMKRMEE KRIPATIDWD DIDSIATEAR QKFKKINPET
IGQASRISGV NPADISILMV YLEGKSRSIS KNQEKTKK
//
