MNMA_HAEIG
ID MNMA_HAEIG Reviewed; 385 AA.
AC A5UFX6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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};
GN OrderedLocusNames=CGSHiGG_03465;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(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}.
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; CP000672; ABQ99681.1; -; Genomic_DNA.
DR AlphaFoldDB; A5UFX6; -.
DR SMR; A5UFX6; -.
DR EnsemblBacteria; ABQ99681; ABQ99681; CGSHiGG_03465.
DR KEGG; hiq:CGSHiGG_03465; -.
DR HOGENOM; CLU_035188_1_0_6; -.
DR OMA; AVCTGHY; -.
DR Proteomes; UP000001990; 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; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..385
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_0000349654"
FT REGION 118..120
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 170..172
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT REGION 332..333
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT ACT_SITE 220
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 149
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT SITE 365
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT DISULFID 123..220
FT /note="Alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ SEQUENCE 385 AA; 43073 MW; 9F3ECA60E2E5FC8F CRC64;
MLISNTYNQH FPQLTQEQIA SNATKKVICG MSGGVDSSVS AFILQQQGYQ VEGLFMKNWE
EDDDDDTDYC TAAADLADAQ AVCDKLGIKL HKINFAAEYW DNVFEHFLTE YKAGRTPNPD
ILCNKEIKFK AFLEYAAEDL GADYIATGHY VRRAGDNENA KLLRGLDANK DQSYFLYTLS
HKQVGQSLFP VGEIEKPIVR AIAEDLGLIT AKKKDSTGIC FIGERKFKDF LARYLPAQPG
NIRTVDDEII GRHDGLMYHT LGQRKGLGIG GLKNAGDEAW YVVDKDVENN ELIVAQGHDH
PRLFSKGLIA SQLHWVDREP IRESLRCTVK TRYRQQDIPC VIEPIDDETI RVIFDEPQSA
VTPGQSAVFY LGEVCLGGGI IAERI
