ID C0E8G4_9FIRM Unreviewed; 352 AA.
AC C0E8G4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 Synonyms=trmU {ECO:0000313|EMBL:EEG32237.1};
GN ORFNames=CLOSTMETH_00109 {ECO:0000313|EMBL:EEG32237.1};
OS [Clostridium] methylpentosum DSM 5476.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=537013 {ECO:0000313|EMBL:EEG32237.1, ECO:0000313|Proteomes:UP000003340};
RN [1] {ECO:0000313|EMBL:EEG32237.1, ECO:0000313|Proteomes:UP000003340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG32237.1,
RC ECO:0000313|Proteomes:UP000003340};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG32237.1, ECO:0000313|Proteomes:UP000003340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5476 {ECO:0000313|EMBL:EEG32237.1,
RC ECO:0000313|Proteomes:UP000003340};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium methylpentosum (DSM 5476).";
RL Submitted (FEB-2009) 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:EEG32237.1}.
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; ACEC01000004; EEG32237.1; -; Genomic_DNA.
DR AlphaFoldDB; C0E8G4; -.
DR STRING; 537013.CLOSTMETH_00109; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_0_0_9; -.
DR Proteomes; UP000003340; 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: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, ECO:0000256|HAMAP-
KW Rule:MF_00144}; Methyltransferase {ECO:0000313|EMBL:EEG32237.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00144}; Reference proteome {ECO:0000313|Proteomes:UP000003340};
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 205..265
FT /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT /evidence="ECO:0000259|Pfam:PF20259"
FT DOMAIN 275..350
FT /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20258"
FT REGION 145..147
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT ACT_SITE 195
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 3..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT SITE 123
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT SITE 334
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT DISULFID 98..195
FT /note="Alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ SEQUENCE 352 AA; 39350 MW; C7401744186E1F14 CRC64;
MIGMSGGVDS SVAAALLIEQ GYEVVGATFR LWKPEDDLFD SEATCCSLDD INDAREVCHQ
LGIPHYVLNL KREFKEAVVQ NFVEEYQAGR TPNPCIVCNQ KIKFDYFYQK AAALGFDYVA
TGHYARIEQN EQGEFQLKTA AYAQKDQSYF LYGIPYPNLG HILFPLGGYT KPQVRELAEK
YGFSVSHKRD SQEICFVDRN GYGTFLERFT GTIPPKGNFI DSQGTVLGEH KGIWHYTVGQ
RKGLGMAFGK PMYVSEINPA DNTVRLVDDE ENYSSRLTAE RMNYLIPHPP SKPVRVQVKI
RNRAEFAPAL LTPLSEAKIE LAFDQPQRAI TKGQSAVLYD GEVCLGGGII TA
//
