ID A0A0A1F8M0_9BURK Unreviewed; 331 AA.
AC A0A0A1F8M0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=LT85_1683 {ECO:0000313|EMBL:AIY40841.1};
OS Collimonas arenae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=279058 {ECO:0000313|EMBL:AIY40841.1, ECO:0000313|Proteomes:UP000030302};
RN [1] {ECO:0000313|EMBL:AIY40841.1, ECO:0000313|Proteomes:UP000030302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cal35 {ECO:0000313|EMBL:AIY40841.1,
RC ECO:0000313|Proteomes:UP000030302};
RA Uroz S., Tech J.J., Sawaya N.A., Frey-Klett P., Leveau J.H.J.;
RT "Structure and function of bacterial communities in ageing soils: insights
RT from the Mendocino ecological staircase.";
RL Soil Biol. Biochem. 69:265-274(2014).
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; CP009962; AIY40841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1F8M0; -.
DR STRING; 279058.LT85_1683; -.
DR KEGG; care:LT85_1683; -.
DR HOGENOM; CLU_016902_1_1_4; -.
DR Proteomes; UP000030302; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:AIY40841.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 22..81
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 309..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 331 AA; 37005 MW; EC4571FADFD34FA3 CRC64;
MQAPPAPLQV QLLTIGEEDA GQRIDNFLLR ICKGVPKSHI YRVLRSGEVR VNKGRIDQTY
RLIEGDVIRV PPIRIAEKQD QMVPGAEFKI LLEDNHMLVI DKPAGVAVHG GSGVSYGVIE
QLRAARPEAK FLELVHRLDR DTSGILLLAK KRSALTNLHE QMREGDTDKR YLVLVHGDWQ
NERQHIKLPL HKYTAADGER RVRVQADGQA SHTIFNLIRR YGDYALLEAE LKTGRTHQIR
VHLSSSGFAI AGDDKYGDFA LNRALQKADG SRIALKRMFL HAYQITFAHP ETGKPITLKA
PLPPECEKFL KSLPDGKSDN VASAPSRTTG D
//
