ID Q2RTX4_RHORT Unreviewed; 349 AA. AC Q2RTX4; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 07-APR-2021, entry version 100. 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 Short=U20-specific Dus {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 4362 / OS 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|EMBL:ABC22421.1, 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}; RX PubMed=21886856; DOI=10.4056/sigs.1804360; RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K., RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C., RA Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y., RA Roberts G.P., Reslewic S., Schwartz D.C.; RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1)."; RL Stand. Genomic Sci. 4:293-302(2011). 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. Specifically modifies U20 and U20a in CC tRNAs. {ECO:0000256|HAMAP-Rule:MF_02041}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + CC uridine(20) in tRNA; Xref=Rhea:RHEA:53340, Rhea:RHEA-COMP:13533, CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02041}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH + CC uridine(20) in tRNA; Xref=Rhea:RHEA:53336, Rhea:RHEA-COMP:13533, CC Rhea:RHEA-COMP:13534, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.91; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02041}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH + CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535, CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02041}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH + CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535, CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02041}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|ARBA:ARBA00001917, CC ECO:0000256|HAMAP-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. {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; YP_426708.1; NC_007643.1. DR STRING; 269796.Rru_A1621; -. DR EnsemblBacteria; ABC22421; ABC22421; Rru_A1621. DR KEGG; rru:Rru_A1621; -. DR PATRIC; fig|269796.9.peg.1698; -. DR eggNOG; COG0042; Bacteria. DR HOGENOM; CLU_013299_2_1_5; -. DR OMA; RVQNNMI; -. DR OrthoDB; 1320183at2; -. DR Proteomes; UP000001929; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0102264; F:tRNA-dihydrouridine20 synthase activity; IEA:UniProtKB-EC. DR CDD; cd02801; DUS_like_FMN; 1. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_02041; DusA_subfam; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR035587; DUS-like_FMN-bd. DR InterPro; IPR001269; DUS_fam. DR InterPro; IPR004653; DusA. DR InterPro; IPR018517; tRNA_hU_synthase_CS. DR PANTHER; PTHR42907; PTHR42907; 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621}; KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_02041, KW ECO:0000256|PIRNR:PIRNR006621}; NADP {ECO:0000256|HAMAP-Rule:MF_02041}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_02041, 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|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_02041, ECO:0000256|PIRNR:PIRNR006621}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02041}. FT DOMAIN 23..323 FT /note="Dus" FT /evidence="ECO:0000259|Pfam:PF01207" FT NP_BIND 25..27 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT NP_BIND 219..221 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT NP_BIND 248..249 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 108 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041, FT ECO:0000256|PIRSR:PIRSR006621-1" FT BINDING 78 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT BINDING 147 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT BINDING 179 FT /note="FMN" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT SITE 105 FT /note="Interacts with tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT SITE 191 FT /note="Interacts with tRNA; defines subfamily-specific FT binding signature" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT SITE 194 FT /note="Interacts with tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT SITE 314 FT /note="Interacts with tRNA; defines subfamily-specific FT binding signature" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02041" FT SITE 317 FT /note="Interacts with tRNA; defines subfamily-specific FT binding signature" FT /evidence="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 //