ID   TSR3_METST              Reviewed;         171 AA.
AC   Q2NET3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Msp_1293;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57670.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NET3; -.
DR   SMR; Q2NET3; -.
DR   STRING; 339860.Msp_1293; -.
DR   EnsemblBacteria; ABC57670; ABC57670; Msp_1293.
DR   KEGG; mst:Msp_1293; -.
DR   eggNOG; arCOG04733; Archaea.
DR   HOGENOM; CLU_035060_4_2_2; -.
DR   OMA; DCSWESA; -.
DR   Proteomes; UP000001931; 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..171
FT                   /note="16S rRNA aminocarboxypropyltransferase"
FT                   /id="PRO_1000065242"
FT   BINDING         18
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         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01116"
FT   BINDING         91
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         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01116"
SQ   SEQUENCE   171 AA;  19416 MW;  85AABE26FC1A66B1 CRC64;
     MMKIVIYHSN ECDPKRCTSI KLQKQNKVAI THNMRKIPYN AIVLDAEADK AVSREDREKI
     TKYGLSALDC SWKKLKKSSF NFKSKKNHRL LPFLVAANPV NYGKPCILSS AEALSAALYI
     VGYKDEARDL MNSFKWGPHF ITLNENLLEA YSEAKNSTEI VEVQNEFLGG K