ID F0ZKX6_DICPU Unreviewed; 402 AA.
AC F0ZKX6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00038890};
DE EC=1.3.1.88 {ECO:0000256|ARBA:ARBA00038890};
GN ORFNames=DICPUDRAFT_152274 {ECO:0000313|EMBL:EGC35390.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC35390.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00035900};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC Evidence={ECO:0000256|ARBA:ARBA00035900};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00036049};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC Evidence={ECO:0000256|ARBA:ARBA00036049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00035864};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC Evidence={ECO:0000256|ARBA:ARBA00035864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00035813};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC Evidence={ECO:0000256|ARBA:ARBA00035813};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038313}.
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DR EMBL; GL871061; EGC35390.1; -; Genomic_DNA.
DR RefSeq; XP_003288066.1; XM_003288018.1.
DR AlphaFoldDB; F0ZKX6; -.
DR STRING; 5786.F0ZKX6; -.
DR EnsemblProtists; EGC35390; EGC35390; DICPUDRAFT_152274.
DR GeneID; 10501501; -.
DR KEGG; dpp:DICPUDRAFT_152274; -.
DR eggNOG; KOG2335; Eukaryota.
DR InParanoid; F0ZKX6; -.
DR OMA; LIYPYVD; -.
DR OrthoDB; 5487726at2759; -.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
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; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 1.
DR PANTHER; PTHR11082:SF5; TRNA-DIHYDROURIDINE(16_17) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001064};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 54..312
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 358..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 46257 MW; 05817B40EAA7D038 CRC64;
MTDIEIKENI ETTINKEEEE ENTETILMNP TTIINKIGGY EFFRNVLKSP KLVVAPMVDH
TYLAFRMLTR KYGADLVYTP MFHSKNFVTC KTYRKDNFTT CPEDRPLVVQ FCGNDPEWVV
KAAKLVEDRC DAIDLNLGCP QQIARRGNYG SFLLDKPHII LPIVRELHKN IKVPIFCKIR
LLPDLKDTIK LALDLQEAGC QLLTVHGRTK EQKGQYSGHA NWDAIRQIKE VLHIPVIANG
SVVKFDDIDR CLEASKADGI MSAEGLLANP SFFCGKDISI YQVAHEYMDF SIQYTTAGHI
VRSHLFKMLK EKFDNYSDLR DKMGETHTID GFRDIVNELE NRYKTGAPFI KCLTNKQKRE
LKEKEDQDKQ ENEKKQKTEN DENLNNNVDN NNNNNSNNTE NK
//
