ID A0A2U1C3B7_9BURK Unreviewed; 337 AA.
AC A0A2U1C3B7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=C8D04_0595 {ECO:0000313|EMBL:PVY55406.1};
OS Simplicispira sp. 125.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2135643 {ECO:0000313|EMBL:PVY55406.1, ECO:0000313|Proteomes:UP000245599};
RN [1] {ECO:0000313|EMBL:PVY55406.1, ECO:0000313|Proteomes:UP000245599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=125 {ECO:0000313|EMBL:PVY55406.1,
RC ECO:0000313|Proteomes:UP000245599};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(1911/1915/1917) in 23S rRNA =
CC pseudouridine(1911/1915/1917) in 23S rRNA; Xref=Rhea:RHEA:42524,
CC Rhea:RHEA-COMP:10097, Rhea:RHEA-COMP:10098, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:65315; EC=5.4.99.23;
CC Evidence={ECO:0000256|ARBA:ARBA00036882};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVY55406.1}.
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DR EMBL; QEKM01000001; PVY55406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1C3B7; -.
DR Proteomes; UP000245599; Unassembled WGS sequence.
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:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 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:UP000245599};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 42..102
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 164
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 337 AA; 36945 MW; 79F836D62FF7EC75 CRC64;
MVGDRQVALD EVSAQDLVED ESPALSETES RVIDMGIAQH GERLDKALAD RVPEFSRSYL
RQLLEHGAVQ LNGHVFFKVA QKVKAGDRVV LEMRPTLESQ AFRPESMAID VVHEDEHLLV
VNKPAGLVVH PAPGNWSGTL LNGLMARDPK SALVPRAGIV HRLDKDTSGL MVVARTRASM
DALVHMIAQR QVHRQYLALA HRPWKAAGSI AVDAPIGRDP RNRLRMAVVD LAMHAGKVAR
TDVELLANGT QVCWVRCTLH TGRTHQIRVH MAFKGHPLVA DGLYGGTSLA GMQRQALHAF
RLAFTHPVTG EAMEFLAPVP TDMRSALDVL GLRYNGA
//