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Database: UniProt
Entry: D0JBJ8_BLASB
LinkDB: D0JBJ8_BLASB
Original site: D0JBJ8_BLASB 
ID   D0JBJ8_BLASB            Unreviewed;       622 AA.
AC   D0JBJ8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   ECO:0000313|EMBL:ACY40536.1};
GN   OrderedLocusNames=BLBBGE_534 {ECO:0000313|EMBL:ACY40536.1};
OS   Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS   germanica symbiotic bacterium).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40536.1, ECO:0000313|Proteomes:UP000002625};
RN   [1] {ECO:0000313|EMBL:ACY40536.1, ECO:0000313|Proteomes:UP000002625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX   PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA   Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA   Latorre A., Moya A.;
RT   "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT   Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL   PLoS Genet. 5:E1000721-E1000721(2009).
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}.
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DR   EMBL; CP001487; ACY40536.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0JBJ8; -.
DR   STRING; 331104.BLBBGE_534; -.
DR   KEGG; bbl:BLBBGE_534; -.
DR   eggNOG; COG0445; Bacteria.
DR   HOGENOM; CLU_007831_2_2_10; -.
DR   OMA; FRPGYAI; -.
DR   Proteomes; UP000002625; 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   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          547..618
FT                   /note="tRNA uridine 5-carboxymethylaminomethyl modification
FT                   enzyme C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01228"
FT   BINDING         12..17
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   622 AA;  71188 MW;  C8EC2F96B49B92CC CRC64;
     MFLDIYDIIV VGGGHAGAEA SLASSNIGSK TLLVTTNLQT IGQMSCNPAI GGIAKGQMVR
     EIDALGGYSG IISDYSMIQF RMLNQSKGPA MWSPRAQCDR KLFSYYWRFF LEKNTQLDLY
     QDTVTSLIIE KNQVKGVKTF FGLKIKGKSV ILTNGTFLNG KIHIGEKKIN GGRIAEQEVR
     GITEQLTKHF GFKYGRMKTG TSPRVDGRSL NYDKMKSQYG DIHPKKFSFF YETKKLTKQR
     KCYITYTNQK VHDLIRKNFN CSPIFTGSIQ GVSPRYCPSI EEKIFRFSDK EEHPIFVEPE
     GWNTVEVYIN GFSTSFSEKI QYQSLKQISG FEKVKILRPG YAIEYDYFPP EQLKPTLESK
     IIENLFFAGQ INGTTGYEEA AAQGLIAGIN ASLKISQKEP FILKRNQAYI GVLIDDLITK
     GTEEPYRMFT SRAEYRMLLR QDNADIRLTP MGYNIGLISE EKMRILDKKK SNIEKCMHLF
     QNRNFEPKVI NPILDDKKSP RIYHDKKIET ILSRSEIDIK DIISIPFLMK EIKNFDQEIL
     EQVSIRIKYK GYIDREKENA KKLLKLENLK IPNNFDYKTI QSLSLEAREK LDYHRPVSLA
     QASRISGVSP SDLSILLIHM GR
//
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