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Database: UniProt
Entry: MNMA_RHIE6
LinkDB: MNMA_RHIE6
Original site: MNMA_RHIE6 
ID   MNMA_RHIE6              Reviewed;         408 AA.
AC   B3PYW4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, 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=RHECIAT_CH0003690;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RX   PubMed=20048063; DOI=10.1128/aem.02039-09;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Fernandez J.L.,
RA   Hernandez Gonzalez I.L., Diaz R., Flores M., Palacios R., Mora J.,
RA   Davila G.;
RT   "Conserved symbiotic plasmid DNA sequences in the multireplicon pangenomic
RT   structure of Rhizobium etli.";
RL   Appl. Environ. Microbiol. 76:1604-1614(2010).
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; CP001074; ACE92628.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PYW4; -.
DR   SMR; B3PYW4; -.
DR   KEGG; rec:RHECIAT_CH0003690; -.
DR   eggNOG; COG0482; Bacteria.
DR   HOGENOM; CLU_035188_0_1_5; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000008817; 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; Adenine nucleotide alpha hydrolases-like domains; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR   InterPro; IPR046885; MnmA-like_C.
DR   InterPro; IPR046884; MnmA-like_central.
DR   InterPro; IPR023382; MnmA-like_central_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR   NCBIfam; TIGR00420; trmU; 1.
DR   PANTHER; PTHR11933:SF5; MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1; 1.
DR   PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR   Pfam; PF03054; tRNA_Me_trans; 1.
DR   Pfam; PF20258; tRNA_Me_trans_C; 1.
DR   Pfam; PF20259; tRNA_Me_trans_M; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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..408
FT                   /note="tRNA-specific 2-thiouridylase MnmA"
FT                   /id="PRO_1000096303"
FT   REGION          172..174
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        222
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         27..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         145
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            146
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            365
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   DISULFID        121..222
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   408 AA;  43848 MW;  DD0BD71C6529B8BF CRC64;
     MSAQNLAPPL NTLDFDKKPE ETRVVVAMSG GVDSSVVAGL LKQQGYDVLG ITLQLYDHGA
     AVHRAGSCCA GQDIDDARRV CETLGIPHYV LDYEKRFRET VINPFAESYV AGETPIPCVS
     CNQTVKFADL LATAKELGAD ALATGHYIRS RPNPSPEHPG RRALFRPADA DRDQSYFLFA
     TTQEQIDYLR FPLGGLPKAE TRRLAEEMGL VVAKKADSQD ICFVPQGKYS DIITKLKPNA
     ALAGEIVHLD GRVLGTHEGI LHFTIGQRRG IGIATGEPLY VVYLDARSRR VIVGPKEALE
     THRVYLRDVN WLGDETLGEA ASGEGFACYA KVRSTRAPAP AVLHVDATGT YVDLTVGEAG
     IAPGQACALY SAPGDDARVF GGGFIERSER EPAAEASLKA LLASPVAA
//
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