ID   TSR3_METS3              Reviewed;         171 AA.
AC   A5UJF3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Msm_0126;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86331.1; -; Genomic_DNA.
DR   RefSeq; WP_004034082.1; NC_009515.1.
DR   AlphaFoldDB; A5UJF3; -.
DR   SMR; A5UJF3; -.
DR   STRING; 420247.Msm_0126; -.
DR   PRIDE; A5UJF3; -.
DR   EnsemblBacteria; ABQ86331; ABQ86331; Msm_0126.
DR   GeneID; 5216792; -.
DR   KEGG; msi:Msm_0126; -.
DR   PATRIC; fig|420247.28.peg.130; -.
DR   eggNOG; arCOG04733; Archaea.
DR   HOGENOM; CLU_035060_4_2_2; -.
DR   OMA; DCSWESA; -.
DR   BioCyc; MSMI420247:GHWZ-127-MON; -.
DR   Proteomes; UP000001992; 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..171
FT                   /note="16S rRNA aminocarboxypropyltransferase"
FT                   /id="PRO_1000065241"
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         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01116"
FT   BINDING         90
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         109
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"
SQ   SEQUENCE   171 AA;  19539 MW;  2EAD391F8092FC39 CRC64;
     MKVTVFHANE CDRKKCTSIK MEKLGKCKLV YNINKIPSGA VVLNPFAQKA VSYEDYRYVH
     RRGVVGLDCS WNEVSSSKKF FSLSKYHRSL PFLIATNPVN YGKPCILSTV EAVSATLYIT
     RFKDEAKDIL DGFKWGHTFL ELNHDLLEAY SEADTSKDVV RVQNEFLESK E