(data stored in SCRATCH zone)

SWISSPROT: MNMC_SALAR

ID   MNMC_SALAR              Reviewed;         666 AA.
AC   A9MJ47;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 72.
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}; OrderedLocusNames=SARI_00521;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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}.
DR   EMBL; CP000880; ABX20447.1; -; Genomic_DNA.
DR   SMR; A9MJ47; -.
DR   PRIDE; A9MJ47; -.
DR   EnsemblBacteria; ABX20447; ABX20447; SARI_00521.
DR   KEGG; ses:SARI_00521; -.
DR   eggNOG; ENOG4105CWG; Bacteria.
DR   eggNOG; COG0665; LUCA.
DR   eggNOG; COG4121; LUCA.
DR   HOGENOM; HOG000218142; -.
DR   KO; K15461; -.
DR   OMA; NFLCAWQ; -.
DR   Proteomes; UP000002084; 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   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
PE   3: Inferred from homology;
DR   PRODOM; A9MJ47.
DR   SWISS-2DPAGE; A9MJ47.
KW   Cytoplasm; FAD; Flavoprotein; Methyltransferase; Multifunctional enzyme;
KW   Oxidoreductase; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..666
FT                   /note="tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
FT                   bifunctional protein MnmC"
FT                   /id="PRO_1000084795"
FT   REGION          1..245
FT                   /note="tRNA (mnm(5)s(2)U34)-methyltransferase"
FT   REGION          270..666
FT                   /note="FAD-dependent cmnm(5)s(2)U34 oxidoreductase"
SQ   SEQUENCE   666 AA;  73780 MW;  A455A8335ADE010B CRC64;
     MKQYAIQPAT LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNRLAE RFPVHSHPLF
     IVAESGFGTG LNFLTLWQAF NNFRSEHPQA TLQRLHFVSF EKFPLTRDDL ALTHQHWPEL
     APWAEQLQAQ WPLPLAGCHR LLLDQGRVTL DLWFGDINEL TDQLDATLNQ KVDAWFLDGF
     APAKNPDMWT PNLFNTMARL ARPGATLATF TSAGFVRRGL QEAGFTMQKR KGFGRKREML
     CGVMERCLTP TISAPWFYRS GSEKRETAII GGGIASALLS LALLRRGWQV TLYCADDKPA
     RGASGNQQGA LYPLLSKHDA AINRFFPTAF TFARRLYDAL PVSFDHDWCG VTQLGWDEKS
     QQKIARMLSL ALPAGLASAL NAEETTQAVG VTTRCGGITY PAGGWLCPEQ LTRAVIALAT
     EQGLQTRFRH TLTSLAAQKS QWQLRFASGE AASHDTVVLA NGHQINRFDQ TQPLPVYAVG
     GQVSHIPTTP ALSALRQVLC YDGYLTPQNP NNRQHCIGAS YHRGNESTVW REEDQRQNRQ
     RLLDCFPDAD WAKEVDVSDN SARCGVRCAT RDHLPMVGNV PDYHATLTHY ADLADNKASA
     VPAPVYPGLF MLGALGSRGL CSAPLCAEIL AAQMSNEPIP LDASTLAALN PNRLWVRKLL
     KGKAVK
//

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