(data stored in SCRATCH9089 zone)

SWISSPROT: MNMC_BURP1

ID   MNMC_BURP1              Reviewed;         660 AA.
AC   Q3JXS0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   11-DEC-2019, entry version 83.
DE   RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC {ECO:0000255|HAMAP-Rule:MF_01102};
DE            Short=tRNA mnm(5)s(2)U biosynthesis bifunctional protein {ECO:0000255|HAMAP-Rule:MF_01102};
DE   Includes:
DE     RecName: Full=tRNA (mnm(5)s(2)U34)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01102};
DE              EC=2.1.1.61 {ECO:0000255|HAMAP-Rule:MF_01102};
DE   Includes:
DE     RecName: Full=FAD-dependent cmnm(5)s(2)U34 oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01102};
DE              EC=1.5.-.- {ECO:0000255|HAMAP-Rule:MF_01102};
GN   Name=mnmC {ECO:0000255|HAMAP-Rule:MF_01102};
GN   OrderedLocusNames=BURPS1710b_0217;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) 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 position
CC       (U34) in tRNA. Catalyzes the FAD-dependent demodification of
CC       cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl
CC       group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form
CC       mnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_01102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-
CC         methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) +
CC         S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19569, Rhea:RHEA-
CC         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:0000255|HAMAP-
CC         Rule:MF_01102};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01102}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC       superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01102}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC       {ECO:0000255|HAMAP-Rule:MF_01102}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABA49513.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000124; ABA49513.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011325005.1; NC_007434.1.
DR   SMR; Q3JXS0; -.
DR   PRIDE; Q3JXS0; -.
DR   EnsemblBacteria; ABA49513; ABA49513; BURPS1710b_0217.
DR   KEGG; bpm:BURPS1710b_0217; -.
DR   HOGENOM; HOG000218143; -.
DR   KO; K15461; -.
DR   OrthoDB; 912110at2; -.
DR   BioCyc; BPSE320372:G1G58-252-MONOMER; -.
DR   Proteomes; UP000002700; Chromosome I.
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   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3JXS0.
DR   SWISS-2DPAGE; Q3JXS0.
KW   Cytoplasm; FAD; Flavoprotein; Methyltransferase; Multifunctional enzyme;
KW   Oxidoreductase; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..660
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_0000347961"
FT   REGION          1..242
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          266..660
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   660 AA;  70759 MW;  F15A2C48EC36CA4B CRC64;
     MTDRIVPATL VFREDGTVVS PLYGDIYHSA AGALAQADHV FIRGNGLPER WRHERAFTII
     ETGFGTGCNF LATWAAWRAD PSHCERLHFV SVEKHPFARE DLRRAAAHIV AYTTITTITP
     IAPLVDELAN AWPALTPGVH RLEFDDGRVT LTLVFGDALD VLPNLALRAH AFYLDGFAPS
     KNADLWSPAI FKSLAKLADE RATFATYTSS GAVKRALDEA GFAYRKVDGF AGKRAMLVGE
     FAPRWRVRRH EPPRAFSTDR RDAIVIGAGL AGCAVVERLA ARGWHVTLIE RRERIASEAS
     GNPAGVFHPM IARDDNLAAR LSRAGFLHAL HRWRALERAG HAFSRSTHGL VQLATSDDEF
     ERMRESIDAL GVPAELASAL SRDDARALLR TDVAHGGWLF AQGGSISPAA LAAAQCAAAG
     DRLSRIVGVE IARLERGGDG RWRALDASGA TIAQASVVVV ANAADAARIA GLRHAPTQRV
     RGQLTLLPPG SAPAVPLPVI GDGYVVPLAN GVTLTGATYE PDDTDATPRE AGHRENLERL
     ERLLPAFSAN ALDAGALAGR VGFRCVASDR LPLVGELGDE AAAAREAAAL TGARLRDVPR
     ATGLYGAFGY GSRGLVWATL GAELIAAQID GEPWPLEREL AEAIDPARFL VRALRHGRVA
//

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