GenomeNet

Database: UniProt
Entry: Q1J2A4_DEIGD
LinkDB: Q1J2A4_DEIGD
Original site: Q1J2A4_DEIGD 
ID   Q1J2A4_DEIGD            Unreviewed;       333 AA.
AC   Q1J2A4;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE            EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
GN   OrderedLocusNames=Dgeo_0077 {ECO:0000313|EMBL:ABF44380.1};
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF44380.1, ECO:0000313|Proteomes:UP000002431};
RN   [1] {ECO:0000313|Proteomes:UP000002431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) 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}.
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; CP000359; ABF44380.1; -; Genomic_DNA.
DR   RefSeq; WP_011529227.1; NC_008025.1.
DR   AlphaFoldDB; Q1J2A4; -.
DR   STRING; 319795.Dgeo_0077; -.
DR   KEGG; dge:Dgeo_0077; -.
DR   eggNOG; COG0042; Bacteria.
DR   HOGENOM; CLU_013299_0_2_0; -.
DR   OMA; RHYTNYF; -.
DR   Proteomes; UP000002431; 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:UP000002431};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR006621}.
FT   DOMAIN          19..313
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ   SEQUENCE   333 AA;  35283 MW;  4D16C717528CCDBB CRC64;
     MICGPGFYAR RLARPGAVLA PMAGYSDAPM RQLAAEQGAL WTVSEMISAR GLVLGGDSEK
     LTLGRPYPGE VGRVVQLFGA EPDVLAQAVA RAESWFAPAA LDLNMGCPVP KVKGRGGACL
     LQTPEVAYTL VRAMRSATTL DVSAKIRLGW DTDRSVEIAQ GLAAAGAALI TVHGRTSVQR
     YSGEADWDAI ARVAASVKVP VVGSGDVKSA EQARARLNTG VAAVMIGRGA VGNPWLFRAL
     ASGDDVVPSA QERARTALRH AQLHVTFYGP DRFGLLSVRP LRKVLPHYLP DHPELRAALV
     QVNTVADVEQ ALAPLLVDAL PPQTQNFVRM SAE
//
DBGET integrated database retrieval system