(data stored in ACNUC7421 zone)

SWISSPROT: MNMA_THEFY

ID   MNMA_THEFY              Reviewed;         363 AA.
AC   Q47SD2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000255|HAMAP-Rule:MF_00144};
DE            EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144};
GN   Name=mnmA {ECO:0000255|HAMAP-Rule:MF_00144};
GN   OrderedLocusNames=Tfu_0597;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble
CC       position (U34) of tRNA, leading to the formation of s(2)U34.
CC       {ECO:0000255|HAMAP-Rule:MF_00144}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] +
CC         uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP +
CC         diphosphate + H(+) + L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131, Rhea:RHEA-
CC         COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC         ChEBI:CHEBI:456215; EC=2.8.1.13; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00144};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00144}.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000255|HAMAP-
CC       Rule:MF_00144}.
DR   EMBL; CP000088; AAZ54635.1; -; Genomic_DNA.
DR   SMR; Q47SD2; -.
DR   STRING; 269800.Tfu_0597; -.
DR   EnsemblBacteria; AAZ54635; AAZ54635; Tfu_0597.
DR   KEGG; tfu:Tfu_0597; -.
DR   eggNOG; ENOG4105CCJ; Bacteria.
DR   eggNOG; COG0482; LUCA.
DR   HOGENOM; HOG000218045; -.
DR   KO; K00566; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01998; tRNA_Me_trans; 1.
DR   Gene3D; 2.30.30.280; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR   InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR   TIGRFAMs; TIGR00420; trmU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SD2.
DR   SWISS-2DPAGE; Q47SD2.
KW   ATP-binding; Complete proteome; Cytoplasm; Disulfide bond;
KW   Nucleotide-binding; Reference proteome; RNA-binding; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN         1    363       tRNA-specific 2-thiouridylase MnmA.
FT                                /FTId=PRO_0000349842.
FT   NP_BIND       8     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00144}.
FT   REGION      145    147       Interaction with tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00144}.
FT   ACT_SITE    103    103       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00144}.
FT   ACT_SITE    195    195       Cysteine persulfide intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00144}.
FT   BINDING      34     34       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00144}.
FT   BINDING     127    127       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00144}.
FT   SITE        128    128       Interaction with tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00144}.
FT   SITE        332    332       Interaction with tRNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00144}.
FT   DISULFID    103    195       Alternate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00144}.
SQ   SEQUENCE   363 AA;  39433 MW;  F69B71AA4321F116 CRC64;
     MTLRVLAAMS GGVDSAVAAA RAVEAGYDVT GVHLALSSNP QSYRTGARGC CTIEDSRDAR
     RAADVIGIPF YIWDMAEEFD RDVVQDFVAE YAAGRTPNPC LRCNEKIKFQ AVLERALALG
     FDAVCTGHHV RLENGRLRRS VDAVKDQSYV LAVLTREQLA HAIFPLGDCT KEEVRAEAAR
     RGLTVADKPD SHDICFIADG DTSGFLERRL GSNPGPIVDE TGQVVGEHRG AHAFTVGQRR
     GLNLSGAPHR RYVLSIEPVS NTVRVGPREA LQVDRIVGER PVWSGCEPPE EWTPFLVQLR
     AHGEVYSCRA RQYEGRVEIL LDEPALGVAK GQAAVLYDGD VVMGSSTIAE TSRVEQAAAN
     HAE
//

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