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Database: UniProt
Entry: A0A1B3PGG9_9BURK
LinkDB: A0A1B3PGG9_9BURK
Original site: A0A1B3PGG9_9BURK 
ID   A0A1B3PGG9_9BURK        Unreviewed;       684 AA.
AC   A0A1B3PGG9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   05-JUN-2019, entry version 19.
DE   RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000256|HAMAP-Rule:MF_01102};
DE            Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000256|HAMAP-Rule:MF_01102};
DE   Includes:
DE     RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102};
DE              EC=2.1.1.61 {ECO:0000256|HAMAP-Rule:MF_01102};
DE   Includes:
DE     RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102};
DE              EC=1.5.-.- {ECO:0000256|HAMAP-Rule:MF_01102};
GN   Name=mnmC {ECO:0000256|HAMAP-Rule:MF_01102,
GN   ECO:0000313|EMBL:AOG21878.1};
GN   ORFNames=BSY15_3040 {ECO:0000313|EMBL:AOG21878.1};
OS   Acidovorax sp. RAC01.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG21878.1, ECO:0000313|Proteomes:UP000094760};
RN   [1] {ECO:0000313|EMBL:AOG21878.1, ECO:0000313|Proteomes:UP000094760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC01 {ECO:0000313|EMBL:AOG21878.1,
RC   ECO:0000313|Proteomes:UP000094760};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the last two steps in the biosynthesis of 5-
CC       methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble
CC       position (U34) in tRNA. Catalyzes the FAD-dependent demodification
CC       of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a
CC       methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form
CC       mnm(5)s(2)U34. {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00015108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC         methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569,
CC         Rhea:RHEA-COMP:10195, Rhea:RHEA-COMP:10197, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74454,
CC         ChEBI:CHEBI:74455; EC=2.1.1.61; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01102, ECO:0000256|SAAS:SAAS01118306};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01102, ECO:0000256|SAAS:SAAS00179145};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00015101}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC       {ECO:0000256|HAMAP-Rule:MF_01102, ECO:0000256|SAAS:SAAS00540894}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-
CC       methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01102,
CC       ECO:0000256|SAAS:SAAS00540888}.
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DR   EMBL; CP016447; AOG21878.1; -; Genomic_DNA.
DR   EnsemblBacteria; AOG21878; AOG21878; BSY15_3040.
DR   KEGG; acra:BSY15_3040; -.
DR   PATRIC; fig|1842533.3.peg.3149; -.
DR   KO; K15461; -.
DR   Proteomes; UP000094760; 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:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro.
DR   GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002097; P:tRNA wobble base modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_01102; MnmC; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR008471; MnmC-like_methylTransf.
DR   InterPro; IPR023032; tRNA_MAMT_biosynth_bifunc_MnmC.
DR   InterPro; IPR017610; tRNA_S-uridine_synth_MnmC_C.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05430; Methyltransf_30; 1.
DR   TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000094760};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423465};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01102, ECO:0000256|SAAS:SAAS00015112};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423462};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00015105};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423464};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00015110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094760};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423457};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423476};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01102,
KW   ECO:0000256|SAAS:SAAS00423459}.
FT   DOMAIN      133    253       Methyltransf_30. {ECO:0000259|Pfam:
FT                                PF05430}.
FT   DOMAIN      279    663       DAO. {ECO:0000259|Pfam:PF01266}.
FT   REGION        1    255       tRNA (mnm(5)s(2)U34)-methyltransferase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01102}.
FT   REGION      281    684       FAD-dependent cmnm(5)s(2)U34
FT                                oxidoreductase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01102}.
SQ   SEQUENCE   684 AA;  72471 MW;  73E6F63A1382D051 CRC64;
     MPGRWLRTPP TRSVREGEGA KRLRGCFISE SIDWLPDGTP YSPRFGDRYH SENGGLEQAS
     GVFLQGCGLP GAWAGQRQWR ILETGFGFGL NFLVTWAAWR ADPQRCGLLH FVSTEAWPVS
     ADDLRRAHAA HPHLADLAHA LHQQWWGLLP GVHRLRFDEG RVLLTLYVGD TQAMLRQQAP
     TVDAVYLDGF SPQRNPDIWD EHTLKAVARC CRRGTRLATW TIARAVRDTL TQCGFEVQRV
     PGVPPKRDNL HAVYAPRWEP RTARGAAVPD VPVAPGRCIV IGGGIAGAAS AASLARRGWQ
     VQVLDAAPAP AAGASALPAG VFAPHVSPDD SVLSRLSRSG VRTTLQQAGW VLAEGTDWSA
     CGVLEHRTDG TPGLPATWSA GSAGAQWSMA APPASLDAAG LPTHTVACWH TRAGWIRPAR
     MVQALLAQPG IAWRGGCAVA QLRRVQPTAA SAAEDDGGVW QVLDAAGHVL AEASHVVIAA
     GAGSSLLLEH RWPLQPVRGQ VSWGLHDGTS PASAVAPFPV NGHGNLVPAF PADWTGGPAA
     PASAPMAWVM GSTFERDVDA LPPSPAEQQA AHTANLAKLH TLLPQAAARL GDAFAAAQQP
     LADDNALPSA VRSWGAIRCT SPDRLPIAGP VDTQALPGLW ACTAMGARGL TLALLCGELL
     AARLHGEPLP LDVRLARALG TERL
//
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