ARLMC_PYRHO
ID ARLMC_PYRHO Reviewed; 412 AA.
AC O58994;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=23S rRNA (uracil(747)-C(5))-methyltransferase;
DE EC=2.1.1.189;
DE AltName: Full=23S rRNA(m5U747)-methyltransferase;
GN OrderedLocusNames=PH1259;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
CC -!- FUNCTION: Catalyzes the formation of 5-methyl-uridine at position
CC equivalent to 747 (m5U747) in 23S rRNA. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(747) in 23S rRNA = 5-
CC methyluridine(747) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42628, Rhea:RHEA-COMP:10154, Rhea:RHEA-COMP:10155,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.189;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; BA000001; BAA30361.1; -; Genomic_DNA.
DR PIR; G71070; G71070.
DR AlphaFoldDB; O58994; -.
DR SMR; O58994; -.
DR STRING; 70601.3257678; -.
DR EnsemblBacteria; BAA30361; BAA30361; BAA30361.
DR KEGG; pho:PH1259; -.
DR eggNOG; arCOG00122; Archaea.
DR OMA; YCGVGGF; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; PTHR11061; 1.
DR Pfam; PF13649; Methyltransf_25; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..412
FT /note="23S rRNA (uracil(747)-C(5))-methyltransferase"
FT /id="PRO_0000162058"
FT ACT_SITE 369
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 302
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 412 AA; 47095 MW; FFB2CDD11EF5B331 CRC64;
MEMRGKITKI NENGLGVLGN ILVPFAYPGD EVEVTETRER FGKIIARDFK LMTPSPLRIP
GKCSHFGKCG GCLWQGLRYR EQLKLKEEIF KRITGIEAEI KGSPRIWYFR NISNFIITVN
GIGFKEFGMP KTVVNIRECP IFSERTPKYL KALKDFLRES NLKPWNWREG DVHYLQVREG
KFTGEVMVNI IAHVPLNYRE ALMEAFNFAD SIYWSLKADK KDDPRGFPTL VLGNEVIREK
VEGITYLIHP SVFFQTNSYA LPLLLKSVEK FCEGSKVLDL YSGIGTLSLY LAKRGFEVTG
VEVNGTSVEM AKRSAEINSI NATFIQGKAE DAELEGYETL IVDPPRKGLK EFSRRIVKKG
PNTLIYVSCN PLRFILDYRN YLSEAYKVDD ALLIDMFPHT PHIEAVIKLV RR
