MNMA_BLOPB
ID MNMA_BLOPB Reviewed; 367 AA.
AC Q492R5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, 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}; Synonyms=trmU;
GN OrderedLocusNames=BPEN_404;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
CC -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation
CC of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is
CC provided by IscS, via a sulfur-relay system. Binds ATP and its
CC substrate tRNAs. {ECO:0000255|HAMAP-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 -!- SUBUNIT: Interacts with TusE. {ECO:0000255|HAMAP-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; CP000016; AAZ41028.1; -; Genomic_DNA.
DR RefSeq; WP_011282937.1; NC_007292.1.
DR AlphaFoldDB; Q492R5; -.
DR SMR; Q492R5; -.
DR STRING; 291272.BPEN_404; -.
DR EnsemblBacteria; AAZ41028; AAZ41028; BPEN_404.
DR KEGG; bpn:BPEN_404; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_1_0_6; -.
DR OMA; AVCTGHY; -.
DR BioCyc; CBLO291272:BPEN_RS01985-MON; -.
DR Proteomes; UP000007794; 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; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..367
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_1000057945"
FT REGION 98..100
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 150..152
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 312..313
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 200
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 129
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 345
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 103..200
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 367 AA; 41756 MW; B89CEEF08EAF232C CRC64;
MSFNHIKKVI VGMSGGVDSS VSAWLLQQQG YKVEGLFMKN WEDDDSTEQC ASASDLSDTH
SVCDNLGIYL HTINFSKEYW ENVFQVFLQE YSVGRTPNPD ILCNKEIKFK YFLEFALQDL
DADLIATGHY VRRVDMNKKT YLIRGVDRNK DQSYFLYTLS YKQLKQCLFP VGTLNKFQVR
NIAKKLNLIT ANKKDSTGIC FIGKRKFKDF ISKYIPIRPG VIIDINGNTI GAHQGVSFYT
LGQRKGLKIG GVKQGNGQPW YVIDKDTSNN TLIAAQGRNH PRLMSIAFIT EQTQWVKRDA
LTSPLHCTVK TRYRHPDIQC QIYPLLNNNL KVILKIPVLA ITPGQSAVFY LKERCLGGGI
ITKIYHC
