ID A0A1F5DKE1_9ARCH Unreviewed; 272 AA.
AC A0A1F5DKE1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DUS-like FMN-binding domain-containing protein {ECO:0000259|Pfam:PF01207};
DE Flags: Fragment;
GN ORFNames=A3K81_03385 {ECO:0000313|EMBL:OGD55618.1};
OS Candidatus Bathyarchaeota archaeon RBG_13_60_20.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797380 {ECO:0000313|EMBL:OGD55618.1, ECO:0000313|Proteomes:UP000177051};
RN [1] {ECO:0000313|EMBL:OGD55618.1, ECO:0000313|Proteomes:UP000177051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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 -!- 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 -!- 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:OGD55618.1}.
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DR EMBL; MEZG01000011; OGD55618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5DKE1; -.
DR STRING; 1797380.A3K81_03385; -.
DR Proteomes; UP000177051; 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 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.
PE 4: Predicted;
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 11..254
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGD55618.1"
SQ SEQUENCE 272 AA; 28838 MW; A232A7E4EE033FB5 CRC64;
SLEIIEGPHV SGVQLVGDEP GAMAQAAAVV ESLGYGYVDI NMGCTVAEVT RTGAGVSLMR
SPEKAVVIAG AVAGAVGIPV TCKMRLGTSS GTVNAIQLSR GLVEAGVSAI TVHGRSGERK
FGLPVDHEGI RAVVEAVDVP VVANGGVFTG KDALEMAQRT GAAAVMPGRG LIGNPWLVTE
ILSAFRGEPY SQPTLDERKK VCLEHLRHLC GYYGEREGAV AMRRVLHEYY HGCKRLTELK
RDALTVTSFS HVEALLDRVY VDGQRLSYGE PR
//
