MNMA_PSEPW
ID MNMA_PSEPW Reviewed; 374 AA.
AC B1JBJ1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=PputW619_3418;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000255|HAMAP-
CC Rule:MF_00144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC Rhea:RHEA-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}.
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DR EMBL; CP000949; ACA73902.1; -; Genomic_DNA.
DR RefSeq; WP_012315256.1; NC_010501.1.
DR AlphaFoldDB; B1JBJ1; -.
DR SMR; B1JBJ1; -.
DR STRING; 390235.PputW619_3418; -.
DR EnsemblBacteria; ACA73902; ACA73902; PputW619_3418.
DR KEGG; ppw:PputW619_3418; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_1_0_6; -.
DR OMA; AVCTGHY; -.
DR OrthoDB; 1054741at2; -.
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;
KW ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..374
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_0000349760"
FT REGION 103..105
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 154..156
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 316..317
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 204
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 133
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 348
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 108..204
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 374 AA; 41510 MW; 0D54603992C64BA3 CRC64;
MTSPALKDPA KTRVIVGMSG GVDSSVSALL LMEQGYQVEG LFMKNWEEDD GTEYCTARED
LADAQAVCDR IGIKLHTANF AAEYWDNVFE HFLEEYKAGR TPNPDILCNR EIKFKAFLDY
ALSLGADLIA TGHYVRRRDT GAVTELLKGL DPNKDQSYFL HAVGGKEIAR TLFPVGELEK
PEVRAIAEKH GLATAKKKDS TGICFIGERR FSDFLKQYLP AQPGEIQTTE GEVIGRHHGL
MYHTIGQRQG LGIGGLKDAG DEPWYVLHKD LTRNVLVVGQ GNEHPWLFSR ALLASEIFWV
NPIDLSSPRT LTAKVRYRQS DQRCTLALTE SGYRAVFDEP QRAVTPGQSV VFYDGEVCLG
GGVIETAEPW SPRA
