DUSAL_SYNY3
ID DUSAL_SYNY3 Reviewed; 334 AA.
AC P72872;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000255|HAMAP-Rule:MF_02041};
DE EC=1.3.1.- {ECO:0000255|HAMAP-Rule:MF_02041};
DE EC=1.3.1.91 {ECO:0000255|HAMAP-Rule:MF_02041};
DE AltName: Full=DusA-like U20-specific dihydrouridine synthase {ECO:0000255|HAMAP-Rule:MF_02041};
DE Short=U20-specific Dus {ECO:0000255|HAMAP-Rule:MF_02041};
DE AltName: Full=tRNA-dihydrouridine synthase 2;
GN Name=dus2; OrderedLocusNames=sll0926;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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. Specifically modifies U20 and U20a in
CC tRNAs. {ECO:0000255|HAMAP-Rule:MF_02041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533,
CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533,
CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02041};
CC -!- SIMILARITY: Belongs to the Dus family. DusA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02041}.
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DR EMBL; BA000022; BAA16888.1; -; Genomic_DNA.
DR PIR; S74737; S74737.
DR AlphaFoldDB; P72872; -.
DR SMR; P72872; -.
DR IntAct; P72872; 1.
DR STRING; 1148.1651962; -.
DR PaxDb; P72872; -.
DR EnsemblBacteria; BAA16888; BAA16888; BAA16888.
DR KEGG; syn:sll0926; -.
DR eggNOG; COG0042; Bacteria.
DR InParanoid; P72872; -.
DR OMA; LIYPYVD; -.
DR PhylomeDB; P72872; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02041; DusA_subfam; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR001269; DUS_fam.
DR InterPro; IPR004653; DusA.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR42907; PTHR42907; 1.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR TIGRFAMs; TIGR00742; yjbN; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; RNA-binding;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..334
FT /note="tRNA-dihydrouridine(20/20a) synthase"
FT /id="PRO_0000162151"
FT ACT_SITE 100
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 17..19
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 70
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 139
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 171
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 211..213
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT BINDING 233..234
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 97
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 183
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 186
FT /note="Interacts with tRNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
FT SITE 302
FT /note="Interacts with tRNA; defines subfamily-specific
FT binding signature"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02041"
SQ SEQUENCE 334 AA; 37929 MW; E5AB3C5E98268719 CRC64;
MTKIFADSSI NPLSVAPMMD HTDRHFRYFL RQLTRHTLLY TEMITAQAIL HGDRQRLLNF
SPEEKPVALQ LGGDDPQLLA ECARIGQDWG YDEINLNVGC PSDRVQSGNF GACLMAQPDL
VAQCVSAMQK AVEIPVTVKH RIGIDHRDSY EDLVHFVEIV ANAGCQRFTV HARKAWLQGL
SPKENRTIPP LRYEDVYQLK KDFPQLLIEI NGGITQTEQI QQHLSHVDAV MVGRAAYENP
YLFATVDRDI YHKTNLVPSR AEIIERMLPY VEERLRHGDR LNQITRHLLS LFNGQPRAKF
WRRTLSDSTL LASAGPELLQ TALQAQKFPG VLVA
