ID F2NTH0_TRES6 Unreviewed; 620 AA.
AC F2NTH0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Tresu_2089 {ECO:0000313|EMBL:AEB14959.1};
OS Treponema succinifaciens (strain ATCC 33096 / DSM 2489 / 6091).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=869209 {ECO:0000313|EMBL:AEB14959.1, ECO:0000313|Proteomes:UP000006852};
RN [1] {ECO:0000313|EMBL:AEB14959.1, ECO:0000313|Proteomes:UP000006852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33096 / DSM 2489 / 6091
RC {ECO:0000313|Proteomes:UP000006852};
RX PubMed=21886863;
RA Han C., Gronow S., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Zeytun A., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Mikhailova N.,
RA Huntemann M., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Treponema succinifaciens type strain (6091).";
RL Stand. Genomic Sci. 4:361-370(2011).
RN [2] {ECO:0000313|Proteomes:UP000006852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33096 / DSM 2489 / 6091
RC {ECO:0000313|Proteomes:UP000006852};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Treponema succinifaciens DSM 2489.";
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=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 -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00005642, ECO:0000256|HAMAP-
CC Rule:MF_01080}.
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DR EMBL; CP002631; AEB14959.1; -; Genomic_DNA.
DR AlphaFoldDB; F2NTH0; -.
DR STRING; 869209.Tresu_2089; -.
DR KEGG; tsu:Tresu_2089; -.
DR eggNOG; COG0130; Bacteria.
DR HOGENOM; CLU_440703_0_0_12; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000006852; Chromosome.
DR GO; GO:0003919; F:FMN adenylyltransferase 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: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 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR032819; TruB_C.
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; PF16198; TruB_C_2; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 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 Isomerase {ECO:0000256|HAMAP-Rule:MF_01080};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006852};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01080}.
FT DOMAIN 34..187
FT /note="Pseudouridine synthase II N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01509"
FT DOMAIN 188..228
FT /note="tRNA pseudouridylate synthase B C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16198"
FT DOMAIN 375..520
FT /note="FAD synthetase"
FT /evidence="ECO:0000259|Pfam:PF06574"
FT ACT_SITE 49
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01080"
SQ SEQUENCE 620 AA; 69230 MW; FD05FD7E119D5B1F CRC64;
MSRMPEKTKN KVSGVMLYAK TPGITSFSSL WSIKHALKTE KVGHTGTLDS FAEGLLVVLS
GNLTHLVPHI TSFTKTYQAV VCFGKETDTL DPTGDVVKTG AAVSKEQIEV ALKKFTGAVL
QVPPVYSALH VDGKRASDLV RGGNEIHLES RQVFVYKNEL LDFKEPSEND ACSYALLEIV
CSKGTYIRAL ARDIAYSLGT CAHLCALRRT KVGPFELKDA ACFGELKEFS IENGIQNAFY
FQKEKEKIHL PFEQKIKKSR EDSAEKIQDI RNHFLLFSQK LASLCGFSCD ILKPEFEKSY
LNGRPLSQKM FDIAICGNVE DEIAVFYSSG AFAGIICKNK DAKLSYGFVV PPEKKEFKVF
SWNEFCSLNF PVEWKSKGCA LTIGSFEAIH AGHVALIKTA VSQKNFVSGI ITFSSQIKNE
GTGLIFTLEQ RLEFFKDLGL DFAVVIDFTQ DFSKIEGADF IETLISVCGM KFLVEGSDFK
CGYKGLLNME ELEKISQKKN FELCRQDYVF FEDEKISSSR VKKEILAGNF ICAQKMLLRP
FALDVRGISF KEKSVGSENS IFEFHNEKNQ VLPKNGIYKV TALDSDGNIF HTTLEIENEN
LRIALPTSGI AEKTAEIKFC
//
