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Database: UniProt
Entry: A0A1Q4WGH4_9ACTN
LinkDB: A0A1Q4WGH4_9ACTN
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ID   A0A1Q4WGH4_9ACTN        Unreviewed;       373 AA.
AC   A0A1Q4WGH4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=A6A06_00250 {ECO:0000313|EMBL:OKI09198.1};
OS   Streptomyces sp. CB02923.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI09198.1, ECO:0000313|Proteomes:UP000185893};
RN   [1] {ECO:0000313|EMBL:OKI09198.1, ECO:0000313|Proteomes:UP000185893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB02923 {ECO:0000313|EMBL:OKI09198.1,
RC   ECO:0000313|Proteomes:UP000185893};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI09198.1}.
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DR   EMBL; LWKZ01000001; OKI09198.1; -; Genomic_DNA.
DR   RefSeq; WP_073757562.1; NZ_LWKZ01000001.1.
DR   AlphaFoldDB; A0A1Q4WGH4; -.
DR   STRING; 1718985.A6A06_00250; -.
DR   OrthoDB; 9800696at2; -.
DR   Proteomes; UP000185893; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00144}; Reference proteome {ECO:0000313|Proteomes:UP000185893};
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          216..282
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like central"
FT                   /evidence="ECO:0000259|Pfam:PF20259"
FT   DOMAIN          290..363
FT                   /note="tRNA-specific 2-thiouridylase MnmA-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20258"
FT   REGION          156..158
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   ACT_SITE        208
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   BINDING         133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            134
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
FT   SITE            347
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   373 AA;  39618 MW;  32BAEF4B723FA83C CRC64;
     MTTDAPRRLR VLAAMSGGVD SAVAAARAAE AGHDVTGVHL ALSENPKSFR TGARGCCTIE
     DSHDARRAAD VIGIPFYVWD LAERFREDVV EDFFAEYEAG RTPNPCLRCN EKIKFAALLD
     KALALGFDAV CTGHYATVVE LPDGGRELHR ASDMAKDQSY VLGVLDDRQL AHAMFPLGDT
     LTTKAEIREE AARRGLFVAK KPDSHDICFI ADGDTQAFLA KRLGTAEGDI VDESGARIGT
     HEGAYGFTIG QRKGLRIGTP APDGKPRYVL DISPVDNTVT VGPVEALDVT ALTAVRPRWC
     GAAPSGPGTY TAQLRAHGGE TEVSAELVDG ELRVAFTEPV RGVAPGQAIV LYDGTRVVGS
     ATIATTDRAR AAA
//
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