ID   TSR3_METTH              Reviewed;         169 AA.
AC   O26654;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=MTH_554;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB85060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB85060.1; ALT_INIT; Genomic_DNA.
DR   PIR; C69173; C69173.
DR   RefSeq; WP_048060842.1; NC_000916.1.
DR   AlphaFoldDB; O26654; -.
DR   SMR; O26654; -.
DR   STRING; 187420.MTH_554; -.
DR   EnsemblBacteria; AAB85060; AAB85060; MTH_554.
DR   GeneID; 1470515; -.
DR   KEGG; mth:MTH_554; -.
DR   PATRIC; fig|187420.15.peg.534; -.
DR   HOGENOM; CLU_035060_4_2_2; -.
DR   OMA; DCSWESA; -.
DR   Proteomes; UP000005223; 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..169
FT                   /note="16S rRNA aminocarboxypropyltransferase"
FT                   /id="PRO_0000094421"
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   169 AA;  18916 MW;  2314126481104C47 CRC64;
     MKIVVYHAEE CDRKKCTSLK LGRKGKFKIV SSLNQLPRGA LVLNPFSEKA VSPEDRDMVL
     RRGIAALDCS WKKVKKSSVI FQTARNHRSL PFLVAANPTN YGKPCILSTA EAVAATLYIV
     GLKDIASDIM SYFKWGPHFL DLNRELLEAY SRAENSLEVV EIQKKFIGG