MNMA_STRPN
ID MNMA_STRPN Reviewed; 373 AA.
AC Q97T38;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE EC=2.8.1.13;
GN Name=mnmA; Synonyms=trmU; OrderedLocusNames=SP_0118;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE.
RG Midwest center for structural genomics (MCSG);
RT "The crystal structure of tRNA (5-methylaminomethyl-2-thiouridylate)-
RT methyltransferase trmU from Streptococcus pneumoniae.";
RL Submitted (AUG-2006) to the PDB data bank.
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000305}.
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DR EMBL; AE005672; AAK74304.1; -; Genomic_DNA.
DR PIR; G95013; G95013.
DR RefSeq; WP_001282969.1; NZ_AKVY01000001.1.
DR PDB; 2HMA; X-ray; 2.41 A; A=1-373.
DR PDBsum; 2HMA; -.
DR AlphaFoldDB; Q97T38; -.
DR SMR; Q97T38; -.
DR STRING; 170187.SP_0118; -.
DR EnsemblBacteria; AAK74304; AAK74304; SP_0118.
DR KEGG; spn:SP_0118; -.
DR eggNOG; COG0482; Bacteria.
DR OMA; AVCTGHY; -.
DR PhylomeDB; Q97T38; -.
DR BioCyc; SPNE170187:G1FZB-123-MON; -.
DR EvolutionaryTrace; Q97T38; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding;
KW RNA-binding; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..373
FT /note="tRNA-specific 2-thiouridylase MnmA"
FT /id="PRO_0000121685"
FT REGION 98..100
FT /note="Interaction with target base in tRNA"
FT /evidence="ECO:0000250"
FT REGION 150..152
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 244..253
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT REGION 312..313
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 128
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT SITE 344
FT /note="Interaction with tRNA"
FT /evidence="ECO:0000250"
FT DISULFID 103..200
FT /note="Alternate"
FT /evidence="ECO:0000250"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 200..204
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2HMA"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:2HMA"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 284..297
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 301..312
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 329..338
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:2HMA"
FT STRAND 353..369
FT /evidence="ECO:0007829|PDB:2HMA"
SQ SEQUENCE 373 AA; 41682 MW; 8C1E1A81603D426F CRC64;
MSDNSKTRVV VGMSGGVDSS VTALLLKEQG YDVIGIFMKN WDDTDENGVC TATEDYKDVV
AVADQIGIPY YSVNFEKEYW DRVFEYFLAE YRAGRTPNPD VMCNKEIKFK AFLDYAITLG
ADYVATGHYA RVARDEDGTV HMLRGVDNGK DQTYFLSQLS QEQLQKTMFP LGHLEKPEVR
RLAEEAGLST AKKKDSTGIC FIGEKNFKNF LSNYLPAQPG RMMTVDGRDM GEHAGLMYYT
IGQRGGLGIG GQHGGDNAPW FVVGKDLSKN ILYVGQGFYH DSLMSTSLEA SQVHFTREMP
EEFTLECTAK FRYRQPDSKV TVHVKGEKTE VIFAEPQRAI TPGQAVVFYD GEECLGGGLI
DNAYRDGQVC QYI
