ID D1P1H0_9GAMM Unreviewed; 216 AA.
AC D1P1H0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=PROVRUST_06041 {ECO:0000313|EMBL:EFB72756.1};
OS Providencia rustigianii DSM 4541.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB72756.1, ECO:0000313|Proteomes:UP000005512};
RN [1] {ECO:0000313|EMBL:EFB72756.1, ECO:0000313|Proteomes:UP000005512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB72756.1,
RC ECO:0000313|Proteomes:UP000005512};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00037305}.
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(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:0000256|ARBA:ARBA00036184};
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:0000256|ARBA:ARBA00036916};
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:EFB72756.1}.
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DR EMBL; ABXV02000021; EFB72756.1; -; Genomic_DNA.
DR AlphaFoldDB; D1P1H0; -.
DR STRING; 500637.PROVRUST_06041; -.
DR eggNOG; COG0564; Bacteria.
DR HOGENOM; CLU_016902_11_1_6; -.
DR Proteomes; UP000005512; Unassembled WGS sequence.
DR GO; GO:0140098; F:catalytic activity, acting on RNA; IEA:UniProt.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 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 NCBIfam; TIGR00005; rluA_subfam; 1.
DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF100; RNA PSEUDOURIDYLATE SYNTHASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU362028, ECO:0000313|EMBL:EFB72756.1}.
FT DOMAIN 20..166
FT /note="Pseudouridine synthase RsuA/RluA-like"
FT /evidence="ECO:0000259|Pfam:PF00849"
FT ACT_SITE 62
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 216 AA; 24877 MW; 610414537FBE9D8E CRC64;
MLPYNPPTDP WLHILYQDEH IIVVNKPSEL LSVPGKAPEH HDSIISRIQR DHPAAESVHR
LDMATSGVMV VALNKAAERE LKRQFREREP KKHYVARVWG HLENKEGLID LPLICDWPNR
PKQKVCFETG KSAQTEYQVL EYEEQATRVK LSPITGRSHQ LRVHMLALGH PILGDRFYAH
EEALALAPRL QLHAQELYIT HPAYGTPMHF TCQPDF
//
