ID E0RV63_BUTPB Unreviewed; 373 AA.
AC E0RV63;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000256|HAMAP-Rule:MF_00144};
DE EC=2.8.1.13 {ECO:0000256|HAMAP-Rule:MF_00144};
GN Name=trmU {ECO:0000313|EMBL:ADL34333.1};
GN Synonyms=mnmA {ECO:0000256|HAMAP-Rule:MF_00144};
GN OrderedLocusNames=bpr_I1596 {ECO:0000313|EMBL:ADL34333.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL34333.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL34333.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001042, ECO:0000256|HAMAP-
CC Rule:MF_00144};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144}.
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000256|HAMAP-
CC Rule:MF_00144}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00144}.
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DR EMBL; CP001810; ADL34333.1; -; Genomic_DNA.
DR RefSeq; WP_013280987.1; NC_014387.1.
DR AlphaFoldDB; E0RV63; -.
DR STRING; 515622.bpr_I1596; -.
DR KEGG; bpb:bpr_I1596; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_0_0_9; -.
DR Proteomes; UP000001299; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; 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:0032259; P:methylation; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00144}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00144};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Methyltransferase {ECO:0000313|EMBL:ADL34333.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00144}; Reference proteome {ECO:0000313|Proteomes:UP000001299};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00144};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00144};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00144};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00144}.
FT DOMAIN 225..285
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 293..368
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
FT REGION 163..165
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT REGION 319..320
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT ACT_SITE 117
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT ACT_SITE 213
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT SITE 142
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT SITE 352
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ SEQUENCE 373 AA; 42214 MW; F3C60C622B031B7C CRC64;
MDGLEFKPVT ETKVEKNTAL IAMSGGVDSS VAAALTLKKG YNCIGCTMRL YENDMVGLDL
LGTCCSIEDT KDARSVCDKL GIDYNIYHYE AEFRDKVIEP FVCSYERGET PNPCIRCNKY
LKFDSLYKRA RELGCDYIVT GHYARIEERD GHFYLLKAKD LNKDQSYVLY DLSEEQLRHT
LFPLGEFTKP EVRAIAEENG FVTSHKSESQ DICFVPDGDY AGMIHRYRGK DYPKGDFVDK
DGNVLGTHDG IINYTIGQRR GLGIPADRRL YVTKLDVENN KVILADNIDL FKREMIIRDF
HWITGSEPTN EFRCQAKIRY KHKEQPASVL PLGEKRARVV FDEAQRAITA GQSAVLYDGD
IVLGGGIIDC VVD
//
