ID A0A0L6I0W4_9MICO Unreviewed; 359 AA.
AC A0A0L6I0W4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=mnmA {ECO:0000256|HAMAP-Rule:MF_00144};
GN ORFNames=AKH00_02095 {ECO:0000313|EMBL:KNY07117.1};
OS Microbacterium sp. GCS4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1692239 {ECO:0000313|EMBL:KNY07117.1, ECO:0000313|Proteomes:UP000037096};
RN [1] {ECO:0000313|Proteomes:UP000037096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCS4 {ECO:0000313|Proteomes:UP000037096};
RA Jones K.J., Moore K., Sambles C., Love J., Studholme D.J., Aves S.J.;
RT "Genome sequencing of alga-associated bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNY07117.1}.
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DR EMBL; LGYE01000001; KNY07117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6I0W4; -.
DR STRING; 1692239.AKH00_02095; -.
DR PATRIC; fig|1692239.3.peg.412; -.
DR Proteomes; UP000037096; Unassembled WGS sequence.
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 {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, ECO:0000256|HAMAP-
KW Rule:MF_00144};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00144};
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 202..266
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 274..344
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
FT REGION 141..143
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT ACT_SITE 192
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT SITE 120
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT SITE 332
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT DISULFID 95..192
FT /note="Alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ SEQUENCE 359 AA; 37781 MW; 0ED3968C33368D24 CRC64;
MSGGVDSAVA AARAVEAGHD VVGVHLALSR AGGTLRTGSR GCCTIEDALD ARRAADVLGI
PFYVWDFSER FRDDVIADFV SEYQAGRTPN PCMRCNEKIK FAALLERAIE LGFDAVCTGH
YATLVQTETG LELHRAADNA KDQSYVLGVL TADQLAHTYF PLGTTPSKAI VRAEAAERGL
SVAQKPDSHD ICFIPDGDTR GWLAEKVGTA TGEIVDRTGA VVGSHEGAHA FTVGQRRGLK
LGVPAPDGKP RFVLEVRPVS NTVVVGPKEA LATREIAGER FSWAGASPVA AEFACDVQIR
AHAEPVPARA TVSDLGVTVV PDGPLDGVAP GQTAVLYVGT RVLGQFTIDR TVSAVPVEA
//
