ID A0A1J5LWU9_9PROT Unreviewed; 329 AA.
AC A0A1J5LWU9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=BM562_05935 {ECO:0000313|EMBL:OIQ32041.1};
OS Alphaproteobacteria bacterium MedPE-SWcel.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1860092 {ECO:0000313|EMBL:OIQ32041.1, ECO:0000313|Proteomes:UP000183546};
RN [1] {ECO:0000313|EMBL:OIQ32041.1, ECO:0000313|Proteomes:UP000183546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE-SWcel {ECO:0000313|EMBL:OIQ32041.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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:OIQ32041.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MPDC01000006; OIQ32041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5LWU9; -.
DR STRING; 1860092.BM562_05935; -.
DR Proteomes; UP000183546; Unassembled WGS sequence.
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; IPR004652; DusB-like.
DR InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR NCBIfam; TIGR00737; nifR3_yhdG; 1.
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.
DR PROSITE; PS01136; UPF0034; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 16..319
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 102
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 329 AA; 34975 MW; 010BC74BA6FAA8E4 CRC64;
MSFSVGPTHL DPPIALAPMA GITDRPFRDL VRSFGAGLVV SEMVASQEMV QAKPGVRERA
ELSADVENTA VQLAGREAYW MAEAARQVAD RGACMIDINM GCPAKKVTNG YSGSALLKAP
DHAISLIEAV VQAVDVPVTL KTRLGWDETN LNAADVARRA QDAGVQMVTI HGRTRCQFYK
GQADWAAIAD IRDAISVPLL ANGDIKDVAD ARKALAQSGA DGVMIGRGAQ GRPWVLAEIA
HAIWGKAAPV IPKGSDLVAM VSIHYEAILR FYGPDLGARV ARKHLGWYMD DAGTPAALRR
EILTAGSAEA VLIRLDDALN CCAQQETAA
//
