RLUA_VIBCH
ID RLUA_VIBCH Reviewed; 245 AA.
AC Q9KP71;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Dual-specificity RNA pseudouridine synthase RluA {ECO:0000250|UniProtKB:P0AA37};
DE EC=5.4.99.28 {ECO:0000250|UniProtKB:P0AA37};
DE EC=5.4.99.29 {ECO:0000250|UniProtKB:P0AA37};
DE AltName: Full=23S rRNA pseudouridine(746) synthase {ECO:0000250|UniProtKB:P0AA37};
DE AltName: Full=Ribosomal large subunit pseudouridine synthase A {ECO:0000250|UniProtKB:P0AA37};
DE AltName: Full=rRNA pseudouridylate synthase A {ECO:0000250|UniProtKB:P0AA37};
DE AltName: Full=rRNA-uridine isomerase A {ECO:0000250|UniProtKB:P0AA37};
DE AltName: Full=tRNA pseudouridine(32) synthase {ECO:0000250|UniProtKB:P0AA37};
GN Name=rluA; OrderedLocusNames=VC_2505;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Dual specificity enzyme that catalyzes the synthesis of
CC pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32
CC in the anticodon stem and loop of transfer RNAs.
CC {ECO:0000250|UniProtKB:P0AA37}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(32) in tRNA = pseudouridine(32) in tRNA;
CC Xref=Rhea:RHEA:42544, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10108,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.28;
CC Evidence={ECO:0000250|UniProtKB:P0AA37};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(746) in 23S rRNA = pseudouridine(746) in 23S rRNA;
CC Xref=Rhea:RHEA:42548, Rhea:RHEA-COMP:10109, Rhea:RHEA-COMP:10110,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.29;
CC Evidence={ECO:0000250|UniProtKB:P0AA37};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE003852; AAF95647.1; -; Genomic_DNA.
DR PIR; G82068; G82068.
DR RefSeq; NP_232134.1; NC_002505.1.
DR RefSeq; WP_001251798.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KP71; -.
DR SMR; Q9KP71; -.
DR STRING; 243277.VC_2505; -.
DR DNASU; 2615169; -.
DR EnsemblBacteria; AAF95647; AAF95647; VC_2505.
DR KEGG; vch:VC_2505; -.
DR PATRIC; fig|243277.26.peg.2386; -.
DR eggNOG; COG0564; Bacteria.
DR HOGENOM; CLU_016902_11_1_6; -.
DR OMA; HVSQSRM; -.
DR BioCyc; VCHO:VC2505-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; rRNA processing; tRNA processing.
FT CHAIN 1..245
FT /note="Dual-specificity RNA pseudouridine synthase RluA"
FT /id="PRO_0000162660"
FT ACT_SITE 64
FT /evidence="ECO:0000250|UniProtKB:P0AA37"
SQ SEQUENCE 245 AA; 28688 MW; 45F8C3B17B4FA7BB CRC64;
MAMTEYNPPK DPWIDVIYED EHIIAANKPS GLLSVPGRPV EHYDSMWARL VDYCPDVKVV
HRLDMSTSGL ILFAKGKHME SALKKQFQYR LTHKIYYARV WGVMEQNEGE VNLPLCCDWP
NRPKQKVCFE EGRDSLTRYQ VVKREEKTTV VRLIPITGRS HQLRVHMQSL GHPIVGDDLY
APPEAVEFAD RLQLHAAELC FYHPRSHWLR TLFVPCDFYP EAEEQILQHF DPERKLPDYK
KLSQD
