ID F5T5Z4_9FIRM Unreviewed; 543 AA.
AC F5T5Z4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=tRNA pseudouridine synthase B {ECO:0000256|HAMAP-Rule:MF_01080};
DE EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE Short=Psi55 synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000256|HAMAP-Rule:MF_01080};
DE AltName: Full=tRNA-uridine isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
GN Name=truB {ECO:0000256|HAMAP-Rule:MF_01080,
GN ECO:0000313|EMBL:EGL36679.1};
GN ORFNames=HMPREF9124_1787 {ECO:0000313|EMBL:EGL36679.1};
OS Oribacterium sp. oral taxon 108 str. F0425.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=904296 {ECO:0000313|EMBL:EGL36679.1, ECO:0000313|Proteomes:UP000003787};
RN [1] {ECO:0000313|EMBL:EGL36679.1, ECO:0000313|Proteomes:UP000003787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0425 {ECO:0000313|EMBL:EGL36679.1,
RC ECO:0000313|Proteomes:UP000003787};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-55 in
CC the psi GC loop of transfer RNAs. {ECO:0000256|HAMAP-Rule:MF_01080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001332};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC Evidence={ECO:0000256|ARBA:ARBA00000372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000256|ARBA:ARBA00000385, ECO:0000256|HAMAP-
CC Rule:MF_01080};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004726}.
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000256|ARBA:ARBA00005201}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00005642, ECO:0000256|HAMAP-
CC Rule:MF_01080}.
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:EGL36679.1}.
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DR EMBL; AFIH01000001; EGL36679.1; -; Genomic_DNA.
DR RefSeq; WP_009428293.1; NZ_AFIH01000001.1.
DR AlphaFoldDB; F5T5Z4; -.
DR STRING; 904296.HMPREF9124_1787; -.
DR eggNOG; COG0130; Bacteria.
DR eggNOG; COG0196; Bacteria.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000003787; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd02064; FAD_synthetase_N; 1.
DR CDD; cd02573; PseudoU_synth_EcTruB; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 2.40.30.30; Riboflavin kinase-like; 1.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR015864; FAD_synthase.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR002606; Riboflavin_kinase_bac.
DR InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
DR NCBIfam; TIGR00083; ribF; 1.
DR NCBIfam; TIGR00431; TruB; 1.
DR PANTHER; PTHR13767:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR Pfam; PF06574; FAD_syn; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR Pfam; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR SUPFAM; SSF82114; Riboflavin kinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01080, ECO:0000313|EMBL:EGL36679.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080}.
FT DOMAIN 415..540
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01080"
SQ SEQUENCE 543 AA; 60959 MW; 160B140E19A59217 CRC64;
MDGIINVNKE AGMTSFDVLR ALKKILREKK MGHAGTLDPM AEGVLLVCVG KATKLVDSLM
SEVKVYRAEL LLGVETDTED STGKRLSEEE NCVTKEEVLS AFHSLLGKRE QIPPMYSAKK
VEGKRLYSMA REGIVIERKP SPIEIFSIEL LSLTEPEPFE GLSCRGKHQR ISFRVKCSKG
TYIRTLCTEI GEKLGTKACM SALTREEVGE FHLKESKTLS EIERYTKEGA LSSFLKPALY
SKVPTVLTFG KFDGVHLGHQ KIFSSVFRIG EEEGLKPAVL SFTMEKGSFF LQGRKEMLST
EDEHFTRLKN AGFQEVYLYP LTMEAARMSP EDFVRIILID ALKVKHLVVG TDCSFGYQGA
GNVEFLKNLQ GKYGFRLTVV DKVLTKSPAG EEVEISSSYI RKALEEGRVE EAAALLGRPY
SINGTVVHGK AIGRSLSFPT ANIFPKEGKL IPKEGVYYTR VMARGEEYDA MTNIGKNPSI
SEENPLTIES HLLNFDKEIY GEKIRISFLE RIREQKRFPN LDALKAQLKE DLLTVEQFRK
DRT
//
