ID A0A1B8ADB7_FUSPO Unreviewed; 510 AA.
AC A0A1B8ADB7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=FPOA_10193 {ECO:0000313|EMBL:OBS18466.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS18466.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS18466.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS18466.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. Specifically modifies U47 in
CC cytoplasmic tRNAs (By similarity). Catalyzes the synthesis of
CC dihydrouridine in some mRNAs, thereby affecting their translation.
CC {ECO:0000256|ARBA:ARBA00033731}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
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}.
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:OBS18466.1}.
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DR EMBL; LYXU01000004; OBS18466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8ADB7; -.
DR STRING; 36050.A0A1B8ADB7; -.
DR OMA; RPWWICQ; -.
DR OrthoDB; 5487726at2759; -.
DR Proteomes; UP000091967; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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 mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 31..273
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 266..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57485 MW; EC1548458F642BBF CRC64;
MTSKENSPAV ERPAKLEGRA FYESIGSPKF IVAPMVDQSE FAWRMLTRSF ISPTEQKSLL
AYTPMLHARL FSQDDKYRKA HFQAVKADGE TPWLDGNPSI DRPLFVQFCA NDPDALLSAA
KQVAPYCDAV DLNLGCPQGI ARKGKYGAFL QEDQDLIFRL INILHEELPV PVTAKIRILD
TKEETLAYAQ NVLKAGASIL TVHGRRREQK GHLTGLAEWQ MIRFLRDSLP KETVIFANGN
ILQEGDIEKC LEATGADGVM SAEGNLSDPA IFTKPPPVGE EGRDYWRGKD GKGGYRVDAV
FRRYMDILHE HVFGNKPPER RPLFMPGDDT EWMKESEVVE EEPPSKKRRK DLGKKGEQGP
NMAAMQPHLF HLLRHFVSKH TDVRDMLGKS RAGDIEAYER VLSAVERKVA EELLEYERTN
GESIAESPLV EGEEDPPETE SSRGTQRRCK RPVWVVQPII RPLPNEALKK GALTMSKKEK
AKSQEKKEQE KQEEKGKQED IKAKDEALAG
//
