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Database: UniProt
Entry: W1S874_9SPHN
LinkDB: W1S874_9SPHN
Original site: W1S874_9SPHN 
ID   W1S874_9SPHN            Unreviewed;       340 AA.
AC   W1S874;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   ORFNames=C100_02990 {ECO:0000313|EMBL:ETI65260.1};
OS   Sphingobium sp. C100.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1207055 {ECO:0000313|EMBL:ETI65260.1, ECO:0000313|Proteomes:UP000018867};
RN   [1] {ECO:0000313|EMBL:ETI65260.1, ECO:0000313|Proteomes:UP000018867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C100 {ECO:0000313|EMBL:ETI65260.1,
RC   ECO:0000313|Proteomes:UP000018867};
RX   PubMed=24482512;
RA   Dong C., Bai X., Lai Q., Xie Y., Chen X., Shao Z.;
RT   "Draft Genome Sequence of Sphingobium sp. Strain C100, a Polycyclic
RT   Aromatic Hydrocarbon-Degrading Bacterium from the Deep-Sea Sediment of the
RT   Arctic Ocean.";
RL   Genome Announc. 2:0-0(2014).
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:ETI65260.1}.
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DR   EMBL; AYOY01000026; ETI65260.1; -; Genomic_DNA.
DR   RefSeq; WP_024018397.1; NZ_AYOY01000026.1.
DR   AlphaFoldDB; W1S874; -.
DR   STRING; 1207055.C100_02990; -.
DR   PATRIC; fig|1207055.3.peg.584; -.
DR   eggNOG; COG0042; Bacteria.
DR   OrthoDB; 9764501at2; -.
DR   Proteomes; UP000018867; 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   Reference proteome {ECO:0000313|Proteomes:UP000018867};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          20..314
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   340 AA;  36755 MW;  CFE3834E5A40EA16 CRC64;
     MRSLSPIFIG PVTIAMPVVL APMTGVTDMP FRTLVRRYGS GLNVTEMIAS AAMIRETRQS
     LQKAAWHPLE EPVSMQLAGC SPVEMAEAAR LNADRGAAII DINMGCPVKK VVNGDAGSAL
     MRDLPLAAAL IKATVDAVDV PVTVKMRMGW DHASLNAPEL AHIAEDLGAK LITVHGRTRN
     QMYKGSADWA FVRKVKDAVT LPVIVNGDIC SIEDADTALE QSGADGVMIG RGAYGRPWLI
     GQVMAWLTDG TRLPDPSLAE QYRVIVEHYH AMLDHYDTHT GVNMARKHIG WYTKGLTGSA
     EFRNAVNKEP DAGTVLDMLA RFYEPLIASG LDAAELRKAA
//
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