(data stored in SCRATCH zone)

SWISSPROT: C5B722_EDWI9

ID   C5B722_EDWI9            Unreviewed;       349 AA.
AC   C5B722;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 55.
DE   RecName: Full=tRNA-dihydrouridine(20/20a) synthase {ECO:0000256|HAMAP-Rule:MF_02041};
DE            EC=1.3.1.- {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=NT01EI_0241 {ECO:0000313|EMBL:ACR67484.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67484.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02041}.
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DR   EMBL; CP001600; ACR67484.1; -; Genomic_DNA.
DR   ProteinModelPortal; C5B722; -.
DR   STRING; 634503.NT01EI_0241; -.
DR   EnsemblBacteria; ACR67484; ACR67484; NT01EI_0241.
DR   KEGG; eic:NT01EI_0241; -.
DR   PATRIC; fig|634503.3.peg.217; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000259834; -.
DR   KO; K05539; -.
DR   OMA; TFIIHAR; -.
DR   OrthoDB; POG091H068N; -.
DR   Proteomes; UP000001485; 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: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; IPR004653; DusA.
DR   InterPro; IPR001269; tRNA_hU_synthase.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR42907:SF2; PTHR42907:SF2; 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;
DR   PRODOM; C5B722.
DR   SWISS-2DPAGE; C5B722.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
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:UP000001485};
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      35     37       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   NP_BIND     229    231       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   NP_BIND     251    252       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   ACT_SITE    117    117       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02041, ECO:0000256|PIRSR:PIRSR006621-
FT                                1}.
FT   BINDING      87     87       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   BINDING     156    156       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   BINDING     189    189       FMN. {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   SITE        114    114       Interacts with tRNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_02041}.
FT   SITE        204    204       Interacts with tRNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_02041}.
FT   SITE        317    317       Interacts with tRNA; defines subfamily-
FT                                specific binding signature.
FT                                {ECO:0000256|HAMAP-Rule:MF_02041}.
FT   SITE        320    320       Interacts with tRNA; defines subfamily-
FT                                specific binding signature.
FT                                {ECO:0000256|HAMAP-Rule:MF_02041}.
SQ   SEQUENCE   349 AA;  38703 MW;  73E5AF51979E7253 CRC64;
     MTQAAHQAVH IEQATGARGR DQAGAFSSQR FSIAPMLDWT DRHCRYFHRL LSRQTLLYTE
     MVTTGAIIHG KGDYLAYCEE EHPLALQLGG SNPADLARCA RLAETRGYDE INLNVGCPSD
     RVQNGRFGAC LMGEAQLVAD CVKAMRDVVS IPVTVKTRIG IDEQDSYPFL CDFIGTVAGQ
     GECDTFIVHA RKAWLSGLSP RENREVPPLD YPRVYRLKQD FPHLTIALNG GVKRLDEARA
     HLQHVDGVMV GREAYHNPGI LAQVDSQLFD ADAAVPDSVA VVRALYPYIG RELAQGTYLG
     HITRHILGLF QGIPGARQWR RHLSENAHRP GAGIDVVEQA LRFVDRRAE
//

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