(data stored in ACNUC7421 zone)

HOGENOM: ECOUM_1_PE1012

ID   ECOUM_1_PE1012                       STANDARD;      PRT;   668 AA.
AC   ECOUM_1_PE1012; E1RT37;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=tRNA 5-methylaminomethyl-2-thiouridine biosynthesis
DE   bifunctional protein mnmC; Short=tRNA mnm(5)s(2)U biosynthesis
DE   bifunctional protein; (ECOUM_1.PE1012).
GN   Name=mnmC; OrderedLocusNames=UM146_05190;
OS   ESCHERICHIA COLI UM146.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=869729;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOUM_1.PE1012.
CC       Escherichia coli (strain UM146) chromosome, complete sequence.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E1RT37_ECOUM
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing 5-methylaminomethyl-2-
CC       thiouridylate.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DAO family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-
CC       methyltransferase family.
CC   -!- GENE_FAMILY: HOG000218142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E1RT37; -.
DR   EMBL; CP002167; ADN70443.1; -; Genomic_DNA.
DR   ProteinModelPortal; E1RT37; -.
DR   SMR; E1RT37; 1-245, 265-306, 409-464.
DR   GenomeReviews; CP002167_GR; UM146_05190.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:HAMAP.
DR   GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0002097; P:tRNA wobble base modification; IEA:HAMAP.
DR   HAMAP; MF_01102; MnmC; 1; -.
DR   InterPro; IPR008471; DUF752.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
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; DUF752; 1.
DR   TIGRFAMs; TIGR03197; MnmC_Cterm; 1.
DR   HOGENOMDNA; ECOUM_1.PE1012; -.
KW   ADN70443.1000068575old_1320000031;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Methyltransferase;
KW   Multifunctional enzyme; Oxidoreductase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
SQ   SEQUENCE   668 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKHYSIQPAN LEFNAEGTPV SRDFDDVYFS NDNGLEETRY VFLGGNHLEA RFPEHPHPLF
     VVAESGFGTG LNFLTLWQAF DQFREAHPQA QLQRLHFISF EKFPLTRADL ALAHQHWPEL
     APWAEQLQAQ WPLPLPGCHR LLLDEGRITL DLWFGDINEL TSQLDDSLNQ KVDAWFLDGF
     APAKNPDMWT QNLFNAMARL ARPGSTLATF TSAGFVRRGL QEAGFTMQKR KGFGRKREML
     CGVMEQTLPL PCSTPWFNRT GSNKQEAAII GGGIASALLS LALLRRGWQV TLYCADEAPA
     LGASGNRQGA LYPLLSKHDE ALNRFFSNAF TFARRFYDLL PVKFDHDWCG VTQLGWDEKS
     QHKIAQMLSM DLPAELAVAV EANAVEQITG VATNCSGITY PQGGWLCPAE LTRNVLKLAQ
     QQGLQIHYQY QLQDLSRKDD GWLLNFAGDQ QATHSVVVLA NGHQISRFSQ TSSLPVYSVA
     GQVSHIPTTP ELAELKQVLC YDGYLTPQNT ANQHHCIGAS YHRGSEETAY SDEDQQQNRQ
     RLIDCFPHAQ WAKEVDVSGK EARCGVRCAT RDHLPMVGNV PDYDATLVEY ASLAEKKDEA
     VSAPVYDDLF MFAALGSRGL CSAPLCAEIL AAQMSEEPIP MDASTLAALN PNRLWVRKLL
     KGKAVKAG
//

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