ID Q7UHX8_RHOBA Unreviewed; 334 AA.
AC Q7UHX8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN Name=rluD {ECO:0000313|EMBL:CAD77839.1};
GN OrderedLocusNames=RB12885 {ECO:0000313|EMBL:CAD77839.1};
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090 {ECO:0000313|EMBL:CAD77839.1, ECO:0000313|Proteomes:UP000001025};
RN [1] {ECO:0000313|EMBL:CAD77839.1, ECO:0000313|Proteomes:UP000001025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1
RC {ECO:0000313|Proteomes:UP000001025};
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil.
CC {ECO:0000256|RuleBase:RU362028}.
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 -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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DR EMBL; BX294155; CAD77839.1; -; Genomic_DNA.
DR RefSeq; NP_870762.1; NC_005027.1.
DR AlphaFoldDB; Q7UHX8; -.
DR STRING; 243090.RB12885; -.
DR EnsemblBacteria; CAD77839; CAD77839; RB12885.
DR KEGG; rba:RB12885; -.
DR PATRIC; fig|243090.15.peg.6245; -.
DR eggNOG; COG0564; Bacteria.
DR HOGENOM; CLU_016902_4_4_0; -.
DR InParanoid; Q7UHX8; -.
DR OrthoDB; 9784108at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00849; PseudoU_synth_2; 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 Lyase {ECO:0000313|EMBL:CAD77839.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001025};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 14..78
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 137
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 334 AA; 37007 MW; 3C400F314EB62823 CRC64;
MMREFVVPES ANGFRIDLFL TQSCDGYSRS QIRDAVQNDG AEVDGRIIRP SYKVKAGQKV
RFRVPPPASD DTVPENIPLD ILYEDDGLVV INKPAGMVVH PARGNWTGTL TSALAFRFQS
LSDVGGPTRP GIVHRLDRDT SGVIVVAKNN AVHLNLAAQW HDRLVQKEYT AITFGRLDRD
RDWIHASIGR HPYQRDKQAI REGHATSKTA STFYEVVERH GRVTRVDVRP KTGRTHQIRV
HLAHIGCPIL CDRLYGGHSE LSRSQIRRLA GTEVATPGVK PTPEGEEILL SRQALHAKAL
TFTNPQTGKE MTLTAPLPPD LQAVLDLLSS DSSL
//
