ID A0A1B3PJY7_9BURK Unreviewed; 316 AA.
AC A0A1B3PJY7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=BSY15_2586 {ECO:0000313|EMBL:AOG23073.1};
OS Acidovorax sp. RAC01.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG23073.1, ECO:0000313|Proteomes:UP000094760};
RN [1] {ECO:0000313|Proteomes:UP000094760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil at
CC positions 955, 2504 and 2580 in 23S ribosomal RNA.
CC {ECO:0000256|ARBA:ARBA00002876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in RNA = a pseudouridine in RNA;
CC Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000256|RuleBase:RU362028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(955/2504/2580) in 23S rRNA =
CC pseudouridine(955/2504/2580) in 23S rRNA; Xref=Rhea:RHEA:42528,
CC Rhea:RHEA-COMP:10099, Rhea:RHEA-COMP:10100, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:65315; EC=5.4.99.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000381};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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DR EMBL; CP016447; AOG23073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B3PJY7; -.
DR STRING; 1842533.BSY15_2586; -.
DR KEGG; acra:BSY15_2586; -.
DR PATRIC; fig|1842533.3.peg.2686; -.
DR Proteomes; UP000094760; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProt.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IEA:UniProt.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR00005; rluA_subfam; 1.
DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF93; PSEUDOURIDYLATE SYNTHASE RPUSD4, MITOCHONDRIAL; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU362028};
KW Reference proteome {ECO:0000313|Proteomes:UP000094760};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 11..69
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 316 AA; 35306 MW; 982F29A4B038E962 CRC64;
MVEVDEDSAG QRLDNFLIRH LKGVPKTHVY RIIRSGEVRI NKGRASADTR VEAGDLVRLP
PVRISDKVAE KAERPAPARE FPILLEDEHL IALDKPAGVA VHGGSGVSFG VIEQLRQARP
QARFLELVHR LDRETSGILL VAKKRSALTH LQDQFRERET GKTYLALVTG TWPANKKVVD
LPLHKYLQAD GERRVRVTTA DDPDGMRSIT LVKVRSTMAA RQAQGLPAMS LLEVTIKTGR
THQIRVHLAS QGHGIVGDDK YGDFDLNKRL QKLGMKRMFL HAWRLQFNHP ATGERVALNA
ELPPELSEFL PPPDKA
//
