ID A0A136JLS1_9BACT Unreviewed; 343 AA.
AC A0A136JLS1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN Name=dus {ECO:0000313|EMBL:KXJ98076.1};
GN ORFNames=UZ19_OD1000795 {ECO:0000313|EMBL:KXJ98076.1};
OS Parcubacteria bacterium OLB19.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1617425 {ECO:0000313|EMBL:KXJ98076.1, ECO:0000313|Proteomes:UP000070365};
RN [1] {ECO:0000313|EMBL:KXJ98076.1, ECO:0000313|Proteomes:UP000070365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB19 {ECO:0000313|EMBL:KXJ98076.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (MAR-2015) 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|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:KXJ98076.1}.
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DR EMBL; JZEL01000027; KXJ98076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136JLS1; -.
DR STRING; 1617425.UZ19_OD1000795; -.
DR PATRIC; fig|1617425.3.peg.804; -.
DR Proteomes; UP000070365; 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; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR11082:SF25; DUS DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 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 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 14..336
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 343 AA; 38469 MW; 22E8DF7FE2803959 CRC64;
MNFWEKLPTP FFVLAPMADV TDAAFRRMIA KYSAHKRADG TIGGPDVMWT EFVSADGLVR
ATPEGREKLM ADLVYDATER PIVAQLFSSD EGHMEYAANL CRELGFDGVD INMGCPDRSI
EKQGCGSAMI RNPESAAKII RAAKKGAKSD EMGGIPVSVK TRLGYNRDQL EEWLPFLLNE
EPAVITVHGR TRKEMSKVPA RWERIGRAVE IRNEIQKENS FKTRIIGNGD ALSLLDARRK
ASLSGADGVM LGRAIFGNPW LFHPDLTIES IPLKNRLNVM LEHTELFVEL LPFKNLAVMK
KHYKAYVKDF SGASELRAKL MEQDSVSNIR EIVEDFLVKN PQL
//
