MNMA_RIPO1
ID MNMA_RIPO1 Reviewed; 349 AA.
AC B7K1G5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=PCC8801_3542;
OS Rippkaea orientalis (strain PCC 8801) (Cyanothece sp. (strain PCC 8801)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX NCBI_TaxID=41431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 8801;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001287; ACK67507.1; -; Genomic_DNA.
DR RefSeq; WP_012596765.1; NC_011726.1.
DR AlphaFoldDB; B7K1G5; -.
DR SMR; B7K1G5; -.
DR STRING; 41431.PCC8801_3542; -.
DR EnsemblBacteria; ACK67507; ACK67507; PCC8801_3542.
DR KEGG; cyp:PCC8801_3542; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_0_0_3; -.
DR OMA; AVCTGHY; -.
DR OrthoDB; 1054741at2; -.
DR Proteomes; UP000008204; 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;
KW ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..349
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_1000198609"
FT REGION 143..145
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 298..299
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 193
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 120
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 331
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 94..193
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 349 AA; 38521 MW; D7FAD9896729E35E CRC64;
MNKVVVGLSG GVDSSVAAAV LHHQGYEVIG LTLWLMKGKG QCCSEGMVDA AFICEQLGIP
HHIVDSRDVF QANIVNYLVS GYEAGITPLP CSQCNRAVKF GPMLNYARQE LGCDRIATGH
YARIRYDEIS QRYQLLRAID RNKDQSYFLY DLSQEMLAGT VFPLGDQTKE DTRRIAAEFD
LKTASKPESQ DLCLIEAHGS MKTFLDQYIH QKEGDIVDLE GKVLGKHQGI HHYTIGQRKG
LGVAAPEPLY VVKLDPIMNQ VIVANRANAG RSDCTVTRLN WVSIAAPSTP IRVETQIRYR
SSAVPVDLIP LEDNRVKLVF DEPEFGITPG QAAVFYDGEI LLGGGIIEL
