ID A0A1Q2CDY8_9ACTN Unreviewed; 383 AA.
AC A0A1Q2CDY8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN ORFNames=RPIT_05085 {ECO:0000313|EMBL:AQP44265.1}, SAMN05428934_101623
GN {ECO:0000313|EMBL:SDY39990.1};
OS Tessaracoccus flavus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1610493 {ECO:0000313|EMBL:AQP44265.1, ECO:0000313|Proteomes:UP000188324};
RN [1] {ECO:0000313|EMBL:AQP44265.1, ECO:0000313|Proteomes:UP000188324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP44265.1,
RC ECO:0000313|Proteomes:UP000188324};
RX PubMed=26869509; DOI=10.1099/ijsem.0.000958;
RA Kumari R., Singh P., Schumann P., Lal R.;
RT "Tessaracoccus flavus sp. nov., isolated from the drainage system of a
RT lindane-producing factory.";
RL Int. J. Syst. Evol. Microbiol. 66:1862-1868(2016).
RN [2] {ECO:0000313|EMBL:SDY39990.1, ECO:0000313|Proteomes:UP000199635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RP1 {ECO:0000313|EMBL:SDY39990.1,
RC ECO:0000313|Proteomes:UP000199635};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AQP44265.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RP1T {ECO:0000313|EMBL:AQP44265.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; CP019605; AQP44265.1; -; Genomic_DNA.
DR EMBL; FNPU01000001; SDY39990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2CDY8; -.
DR STRING; 1610493.RPIT_05085; -.
DR KEGG; tfl:RPIT_05085; -.
DR OrthoDB; 9764501at2; -.
DR Proteomes; UP000188324; Chromosome.
DR Proteomes; UP000199635; 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 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.
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:UP000188324};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 26..330
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 383 AA; 41419 MW; C3C7F7079078DC05 CRC64;
MPTIEPLRLH APSRRDAVVV ELPVVLAPMA GVTNAAYRQL CREQGAGLYV CEMITSRGLV
VGDPKTRAML AFDPGEATRS VQLYGVDADV MADAARILIT EHQVDHIDLN FGCPVPKVTR
KGGGGVLPYK RDRLRAIVRE TVRAADEFGV PVTIKTRIGI DDAHVTFLDA GRIAQEEGAA
AIALHGRTVQ QAYSGEADWS RIAELVEEVD IPVLGNGDIW EAEDALRMMD ETGCAGVVIG
RGCLGRPWLF GDLAAAMHGE PLRHRPTLGE VGAMIVRHAE LLSGIMGERH GLTDLRKHMA
WYFKGYPVGE LRRHFAMVSS MAELLALVEQ LDADAEFPVG ELGTPRGRQG SPRGKVVLPY
GWYDDTSGSD LDLSEAEIGV SGG
//
