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Entry: A0A288DFU0_9BACT
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ID   A0A288DFU0_9BACT        Unreviewed;       316 AA.
AC   A0A288DFU0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-JUN-2023, entry version 19.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   ORFNames=P148_SR1C00001G0660 {ECO:0000313|EMBL:AHB41451.1};
OS   candidate division SR1 bacterium RAAC1_SR1_1.
OC   Bacteria; Candidatus Absconditabacteria.
OX   NCBI_TaxID=1394709 {ECO:0000313|EMBL:AHB41451.1, ECO:0000313|Proteomes:UP000217256};
RN   [1] {ECO:0000313|EMBL:AHB41451.1, ECO:0000313|Proteomes:UP000217256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAAC1_SR1_1 {ECO:0000313|EMBL:AHB41451.1,
RC   ECO:0000313|Proteomes:UP000217256};
RA   Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA   Castelle C.J., Thomas B.C., Banfield J.F.;
RT   "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT   four candidate phyla.";
RL   Submitted (NOV-2013) 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|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CP006913; AHB41451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A288DFU0; -.
DR   STRING; 1394709.P148_SR1C00001G0660; -.
DR   KEGG; srb:P148_SR1C001G0660; -.
DR   HOGENOM; CLU_013299_0_3_0; -.
DR   Proteomes; UP000217256; Chromosome.
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   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|PIRNR:PIRNR006621};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006621};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217256};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          8..301
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   316 AA;  35976 MW;  839EC451D9461CE0 CRC64;
     MKPIIGFAPM DGFTDAACRS IAQDIRNEYG DKNQYDFFLW TEFMTADGFV RNREGVIHHL
     ETTPNQKNLI AQIFGGNEET LLQTAKTLDK EYKNRFVGIE LNMGCPANNV MKSGGGAELI
     KDKKRSLEII KNIRKAIDMP FSIKTRTGIN EQDKLNQMEF LLQASPYVDM ITIHARTTAQ
     GYGPNPDRNF IYQLKEQLPN QKIIGNGGIT NYEDIETMRG NLDGVMIGQA AIGNPWIFTP
     HHPTSQEKLT TILKHIELIK NFSTEENLAR SLMEFRKHLY SYVKGIPGSK EFKTTCNSLK
     DYHLLVDHIT NFFFGL
//
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