ID A0A1Q6F865_9BACT Unreviewed; 302 AA.
AC A0A1Q6F865;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=tRNA dihydrouridine synthase DusB {ECO:0000313|EMBL:OKY95099.1};
DE Flags: Fragment;
GN ORFNames=BHV65_11080 {ECO:0000313|EMBL:OKY95099.1};
OS Alistipes sp. 58_9_plus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1896970 {ECO:0000313|EMBL:OKY95099.1, ECO:0000313|Proteomes:UP000186889};
RN [1] {ECO:0000313|EMBL:OKY95099.1, ECO:0000313|Proteomes:UP000186889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58_9_plus {ECO:0000313|EMBL:OKY95099.1};
RX PubMed=27819664; DOI=10.1038/nbt.3704;
RA Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.;
RT "Measurement of bacterial replication rates in microbial communities.";
RL Nat. Biotechnol. 34:1256-1263(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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OKY95099.1}.
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DR EMBL; MNQG01000130; OKY95099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q6F865; -.
DR Proteomes; UP000186889; 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 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 14..295
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
FT NON_TER 302
FT /evidence="ECO:0000313|EMBL:OKY95099.1"
SQ SEQUENCE 302 AA; 33757 MW; B757AB5F8401672B CRC64;
MKIADIELGE KPLLLAPMED VTDPSFRYMC KRFGADVVYT EFISSDGLIR DAAKSLKKLE
IDAAERPVGI QLYGHLIEPM VEAARMAEAA GPDIIDINFG CPVKKIAGRG AGSGMMRDVP
LMVEMTRRIV QAVRKPVTVK TRLGWDEESK NIEEIALRLQ DVGIAALTVH GRTRAQMYRG
EADWTLIGKV KNNPQIHIPI IGNGDVDSGP KAAEMFDRYG VDGVMIGRAT YGRPWIFREV
KHYLATGEVL PQPSVCERVE IAKEHLRKSL EVKGEFVGIL EMRRHLSNYF KGLPDFKPTR
LK
//
