ID Q2RTX4_RHORT Unreviewed; 349 AA. AC Q2RTX4; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 02-NOV-2016, entry version 76. DE RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000256|HAMAP-Rule:MF_02041}; DE EC=1.3.1.91 {ECO:0000256|HAMAP-Rule:MF_02041}; DE AltName: Full=U20-specific dihydrouridine synthase {ECO:0000256|HAMAP-Rule:MF_02041}; DE AltName: Full=tRNA-dihydrouridine synthase A {ECO:0000256|HAMAP-Rule:MF_02041}; GN Name=dusA {ECO:0000256|HAMAP-Rule:MF_02041}; GN OrderedLocusNames=Rru_A1621 {ECO:0000313|EMBL:ABC22421.1}; OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG OS 4362 / NCIB 8255 / S1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Rhodospirillum. OX NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC22421.1, ECO:0000313|Proteomes:UP000001929}; RN [1] {ECO:0000313|Proteomes:UP000001929} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1 RC {ECO:0000313|Proteomes:UP000001929}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., RA Reslewic S., Zhou S., Schwartz D.C.; RT "Complete sequence of the chromosome of Rhodospirillum rubrum ATCC RT 11170."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a CC modified base found in the D-loop of most tRNAs, via the reduction CC of the C5-C6 double bond in target uridines. Specifically modifies CC U20 and U20a in tRNAs. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20) in tRNA + NAD(P)(+) = CC uracil(20) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: 5,6-dihydrouracil(20a) in tRNA + NAD(P)(+) = CC uracil(20a) in tRNA + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP- CC Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621}; CC -!- SIMILARITY: Belongs to the Dus family. DusA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- SIMILARITY: Belongs to the dus family. CC {ECO:0000256|PIRNR:PIRNR006621}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000230; ABC22421.1; -; Genomic_DNA. DR RefSeq; WP_011389311.1; NC_007643.1. DR RefSeq; YP_426708.1; NC_007643.1. DR ProteinModelPortal; Q2RTX4; -. DR STRING; 269796.Rru_A1621; -. DR EnsemblBacteria; ABC22421; ABC22421; Rru_A1621. DR GeneID; 3835038; -. DR KEGG; rru:Rru_A1621; -. DR PATRIC; 23326888; VBIRhoRub82919_1698. DR eggNOG; ENOG4105CEH; Bacteria. DR eggNOG; COG0042; LUCA. DR HOGENOM; HOG000259834; -. DR KO; K05539; -. DR OMA; EQDSYEF; -. DR OrthoDB; POG091H068N; -. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02041; DusA_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004653; DusA. DR InterPro; IPR001269; tRNA_hU_synthase. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR PIRSF; PIRSF006621; Dus; 1. DR TIGRFAMs; TIGR00742; yjbN; 1. DR PROSITE; PS01136; UPF0034; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001929}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621}; KW NADP {ECO:0000256|HAMAP-Rule:MF_02041}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; KW Reference proteome {ECO:0000313|Proteomes:UP000001929}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 25 27 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 219 221 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT NP_BIND 248 249 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT ACT_SITE 108 108 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_02041, ECO:0000256|PIRSR:PIRSR006621- FT 1}. FT BINDING 78 78 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT BINDING 147 147 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT BINDING 179 179 FMN. {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 105 105 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02041}. FT SITE 191 191 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 194 194 Interacts with tRNA. {ECO:0000256|HAMAP- FT Rule:MF_02041}. FT SITE 314 314 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. FT SITE 317 317 Interacts with tRNA; defines subfamily- FT specific binding signature. FT {ECO:0000256|HAMAP-Rule:MF_02041}. SQ SEQUENCE 349 AA; 37800 MW; 8697330561D649F3 CRC64; MMVSAPAPRS QPDRSQPDRR LSVAPMMDWT DRHDRWFLRQ ITKRTLLYTE MITAQALLHA DPGRFLDHHP DEHPLALQLG GSDPRALAEA TRLAAPFGFA EINLNVGCPS DRVSSGRFGA CLMADPALVA ECLSAMAEAS NAPVTIKHRI GIDDLDSYDQ LVGFVDQVAR SGIATIIVHA RKAWLKGLSP KENREIPPLR HDVVHRLKAD FPGLEVILNG GITTLTQALD HLGSGDPAAP AVDGVMIGRA AYETPYMLAQ ADGLIFGEAT PAPSRHEVAL ALLPYLDAMT ARGEPVKRLT RHILGLFHGQ PGARAYRRHL GEAGVRPDAT AQVLIDALAH IPALDEAES //