MNMA1_SYNAS
ID MNMA1_SYNAS Reviewed; 372 AA.
AC Q2LWA6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA 1 {ECO:0000255|HAMAP-Rule:MF_00144};
DE EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144};
GN Name=mnmA1 {ECO:0000255|HAMAP-Rule:MF_00144};
GN OrderedLocusNames=SYNAS_24870; ORFNames=SYN_01256;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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}.
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DR EMBL; CP000252; ABC78366.1; -; Genomic_DNA.
DR RefSeq; WP_011418385.1; NC_007759.1.
DR AlphaFoldDB; Q2LWA6; -.
DR SMR; Q2LWA6; -.
DR STRING; 56780.SYN_01256; -.
DR EnsemblBacteria; ABC78366; ABC78366; SYN_01256.
DR KEGG; sat:SYN_01256; -.
DR eggNOG; COG0482; Bacteria.
DR HOGENOM; CLU_035188_0_0_7; -.
DR OMA; VHLLCEQ; -.
DR OrthoDB; 1054741at2; -.
DR Proteomes; UP000001933; 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;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..372
FT /note="tRNA-specific 2-thiouridylase MnmA 1"
FT /id="PRO_0000349836"
FT REGION 164..166
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 214
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 143
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 348
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 118..214
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 372 AA; 41427 MW; AEB5935DAB3CF31A CRC64;
MISVMAPGSE KTGKVETILK KRVLLAISGG VDSSVAALLL KEEGYEVAGV TMCLGVREEE
NKVRCCGREA IEDARGVCEI LGIPHYVLDY APLLETCVID KFVREYRLGR TPNPCIDCNR
YLKFGHLLDS ARTMGFDYLA TGHYAKIERK ESRWILKKAK DLVKDQTYFL YPIPVAALEH
ILFPLADRTK DEVREIARQA LLPIAEKPES QDLCFVTQDS YRDFLQEQGC PVHPGPIVDR
SGRVLGEHSG TVFYTIGQRH GLGISSPFPL YVVAIDVAGN SVIVSGKEDV YAQGLVAGEM
NWLTPERPQE AEARIRHRKR TCSCRIVPEG DRIRVYFAED QDAVTPGQAV VLYQEDEVLG
GGVIEEALHY AN
