TSR3_SULIK
ID TSR3_SULIK Reviewed; 166 AA.
AC C4KHW1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=16S rRNA aminocarboxypropyltransferase {ECO:0000255|HAMAP-Rule:MF_01116, ECO:0000305};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01116};
GN OrderedLocusNames=M164_1574;
OS Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=426118;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.4 / Kamchatka #3;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the
CC aminocarboxypropyl transfer on pseudouridine corresponding to position
CC 914 in M.jannaschii 16S rRNA. It constitutes the last step in
CC biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-
CC carboxypropyl) pseudouridine (m1acp3-Psi). {ECO:0000255|HAMAP-
CC Rule:MF_01116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(1)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L-
CC methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3-
CC carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:63296, Rhea:RHEA-COMP:11634, Rhea:RHEA-
CC COMP:16310, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01116};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01116}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01116}.
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DR EMBL; CP001402; ACR42175.1; -; Genomic_DNA.
DR RefSeq; WP_012711570.1; NC_012726.1.
DR AlphaFoldDB; C4KHW1; -.
DR SMR; C4KHW1; -.
DR EnsemblBacteria; ACR42175; ACR42175; M164_1574.
DR GeneID; 7810913; -.
DR GeneID; 7940929; -.
DR GeneID; 8761615; -.
DR KEGG; sid:M164_1574; -.
DR HOGENOM; CLU_035060_4_1_2; -.
DR OMA; DCSWESA; -.
DR BioCyc; SISL426118:GI01-1618-MON; -.
DR Proteomes; UP000001479; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; IEA:InterPro.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01116; TSR3; 1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR InterPro; IPR022968; Tsr3-like.
DR InterPro; IPR007177; Tsr3_C.
DR PANTHER; PTHR20426; PTHR20426; 1.
DR Pfam; PF04034; Ribo_biogen_C; 1.
DR Pfam; PF04068; RLI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..166
FT /note="16S rRNA aminocarboxypropyltransferase"
FT /id="PRO_1000213600"
FT BINDING 17
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22, ECO:0000255|HAMAP-
FT Rule:MF_01116"
FT BINDING 103
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01116"
SQ SEQUENCE 166 AA; 19314 MW; 7C0B57F3EA78D6EB CRC64;
MKVYVIDYHK DDPKKCTGRK LVKLKLAELT RVGRGIILNP FSERTLSIND KDILIKSGIT
IIDTSWNNTS QNEFKNVRGE HRRLPILFAG NPIHYGIAYK LSSLEALMAT LYILDEVKEA
IKFSNVVKWG HTFIELNKEL LEAYRNKDEE EIKKIEKEII EKILRK
