ID MNMA_AROAE Reviewed; 374 AA.
AC Q5P7R7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
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}; OrderedLocusNames=AZOSEA05220;
GN ORFNames=ebA986;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR555306; CAI06644.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5P7R7; -.
DR SMR; Q5P7R7; -.
DR STRING; 76114.ebA986; -.
DR KEGG; eba:ebA986; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_1_0_4; -.
DR Proteomes; UP000006552; 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;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..374
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_0000349518"
FT REGION 101..103
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 156..158
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 324..325
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 206
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 131
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 357
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 106..206
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 374 AA; 41661 MW; AC5CE70DC507ED25 CRC64;
MSSNTDPNGM KVVVGMSGGV DSSVTALLLK QQGFDVTGLF MKNWEDDDDD EYCSTRQDLV
DVASVCDVIG IDLEVVNFSA EYKDRVFADF LREYEAGRTP NPDVLCNSEI KFRCFLDHAM
ALGADRIATG HYAQVREWAN DGRSEYQLLK AEDGTKDQSY FLYRLNQAQL AKTLFPLGAL
YKRDVRRIAA EAGLHVAEKK DSTGICFIGE RPFREFLMRY LPMRPGEIRN LDDGRVIGEH
QGLMYHTIGQ RKGLHIGGIK GRQDGAGEHD AWYVAGKDVK ANVLYAVQGH EHPALLKTRL
SATDLHWIAG RDPHTHWVYT AKPRYRTPDM PCEIEALVDG GAEIVFAEPQ WALTPGQSVV
VYESKVCLGG GVIA
//
