ID E6W076_DESIS Unreviewed; 324 AA.
AC E6W076;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN OrderedLocusNames=Selin_0449 {ECO:0000313|EMBL:ADU65202.1};
OS Desulfurispirillum indicum (strain ATCC BAA-1389 / DSM 22839 / S5).
OC Bacteria; Chrysiogenota; Chrysiogenetes; Chrysiogenales; Chrysiogenaceae;
OC Desulfurispirillum.
OX NCBI_TaxID=653733 {ECO:0000313|EMBL:ADU65202.1, ECO:0000313|Proteomes:UP000002572};
RN [1] {ECO:0000313|EMBL:ADU65202.1, ECO:0000313|Proteomes:UP000002572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1389 / DSM 22839 / S5
RC {ECO:0000313|Proteomes:UP000002572};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Haggblom M., Rauschenbach I.,
RA Bini E., Woyke T.;
RT "Complete sequence of Desulfurispirillum indicum S5.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified
CC base found in the D-loop of most tRNAs, via the reduction of the C5-C6
CC double bond in target uridines. {ECO:0000256|ARBA:ARBA00002790,
CC ECO:0000256|PIRNR:PIRNR006621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:54452, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00001387};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in tRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00001183};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR EMBL; CP002432; ADU65202.1; -; Genomic_DNA.
DR RefSeq; WP_013505091.1; NC_014836.1.
DR AlphaFoldDB; E6W076; -.
DR STRING; 653733.Selin_0449; -.
DR KEGG; din:Selin_0449; -.
DR eggNOG; COG0042; Bacteria.
DR HOGENOM; CLU_013299_0_3_0; -.
DR InParanoid; E6W076; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000002572; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR PANTHER; PTHR45846; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR PANTHER; PTHR45846:SF1; TRNA-DIHYDROURIDINE(47) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|PIRNR:PIRNR006621};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000002572};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 18..319
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 324 AA; 35695 MW; 2F9AD6190493EE40 CRC64;
MFHPLQLRHN TIDTPLFMAP VAGVCNIPFR VIAREQGCPN IFTEMVSSEA LSRHIPKTVE
FLRVGAEERL RPFVQLFGAN PATMAQSARI CTEEGFTLID INMGCPVKKV VRSGSGVELM
QHPQLAGEIV SQMVAAAGAC ADITVKTRLG LIHGDELLPE LALQVQQAGA SMLTVHARTR
SDGFGGQARW HEVAPIKSLL HIPLIINGDI TDYPSACLAM EQSRADGAMI AREGYTRPWI
FREILSQVRG QATCEPTPRQ IREILLRHLD LLCQYMPERA HILMRKHGSW YSKGTPGSSE
FRQALNSCTD SAQVRSLIST FAAS
//
