TSR3_METBU
ID TSR3_METBU Reviewed; 173 AA.
AC Q12ZL9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Mbur_0088;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(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; CP000300; ABE51107.1; -; Genomic_DNA.
DR RefSeq; WP_011498271.1; NC_007955.1.
DR AlphaFoldDB; Q12ZL9; -.
DR SMR; Q12ZL9; -.
DR STRING; 259564.Mbur_0088; -.
DR EnsemblBacteria; ABE51107; ABE51107; Mbur_0088.
DR GeneID; 3996774; -.
DR KEGG; mbu:Mbur_0088; -.
DR HOGENOM; CLU_035060_4_1_2; -.
DR OMA; DCSWESA; -.
DR OrthoDB; 113131at2157; -.
DR Proteomes; UP000001979; 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; Reference proteome; Ribosome biogenesis; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..173
FT /note="16S rRNA aminocarboxypropyltransferase"
FT /id="PRO_1000065240"
FT BINDING 25
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 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01116"
FT BINDING 96
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 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01116"
SQ SEQUENCE 173 AA; 20066 MW; A750A079C8194E26 CRC64;
MKKQIDKDYH LHIFHAKQCD PKKCTGKKMA RFELARIFDK VQKIPRGSIL LDPMAKQALS
PADKHEQNIT VLDCSWETVE EVFPHLMRLH LQHRALPYLV ATNPVNFGRP FKLTSVEAFA
AALYILGNKK QAEKILSKFN WGHVFLDMNK EPLEDYSKAK DSNEIIKIQS EYM
