ID   TSR3_METMA              Reviewed;         173 AA.
AC   Q8PSK5;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=MM_3074;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32770.1; -; Genomic_DNA.
DR   RefSeq; WP_011034972.1; NC_003901.1.
DR   AlphaFoldDB; Q8PSK5; -.
DR   SMR; Q8PSK5; -.
DR   STRING; 192952.MM_3074; -.
DR   PRIDE; Q8PSK5; -.
DR   EnsemblBacteria; AAM32770; AAM32770; MM_3074.
DR   GeneID; 24864729; -.
DR   KEGG; mma:MM_3074; -.
DR   PATRIC; fig|192952.21.peg.3564; -.
DR   eggNOG; arCOG04733; Archaea.
DR   HOGENOM; CLU_035060_4_1_2; -.
DR   OMA; DCSWESA; -.
DR   Proteomes; UP000000595; 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_0000094420"
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;  19894 MW;  C9DA9A3922ADF07E CRC64;
     MNQTKSRDIP LYIYHAGQCD PKKCTGRKMA RFELARLYDR ISRLPRSAIL LDPMAEKALS
     PADDPKKGII VLDCSWEEVE RVFPELEKLN LEHRALPYML AGNPVNFGRP FKLNSAEAFA
     AALYILGYKE QAEKVMSKFN WGHSFLELNR EPLEEYSTAK NSTEIVEIQS HYI