(data stored in SCRATCH zone)

SWISSPROT: Q3KIP7_PSEPF

ID   Q3KIP7_PSEPF            Unreviewed;       336 AA.
AC   Q3KIP7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=tRNA-dihydrouridine synthase B {ECO:0000256|HAMAP-Rule:MF_02042};
DE            EC=1.3.1.- {ECO:0000256|HAMAP-Rule:MF_02042};
GN   Name=dusB {ECO:0000256|HAMAP-Rule:MF_02042};
GN   OrderedLocusNames=Pfl01_0615 {ECO:0000313|EMBL:ABA72359.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72359.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72359.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72359.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_02042, 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,
CC         Rhea:RHEA-COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02042};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5,6-dihydrouridine in tRNA + NADP(+) = a uridine in
CC         tRNA + H(+) + NADPH; Xref=Rhea:RHEA:23624, Rhea:RHEA-COMP:13339,
CC         Rhea:RHEA-COMP:13887, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02042};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621};
CC   -!- SIMILARITY: Belongs to the Dus family. DusB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02042}.
CC   -!- SIMILARITY: Belongs to the dus family.
CC       {ECO:0000256|PIRNR:PIRNR006621}.
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DR   EMBL; CP000094; ABA72359.1; -; Genomic_DNA.
DR   RefSeq; WP_011332261.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0615; -.
DR   EnsemblBacteria; ABA72359; ABA72359; Pfl01_0615.
DR   KEGG; pfo:Pfl01_0615; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217855; -.
DR   KO; K05540; -.
DR   OMA; RPWLFAD; -.
DR   BioCyc; PFLU205922:G1G4S-623-MONOMER; -.
DR   Proteomes; UP000002704; 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:0017150; F:tRNA dihydrouridine synthase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_02042; DusB_subfam; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR032887; DusB.
DR   InterPro; IPR024036; tRNA-dHydroUridine_Synthase_C.
DR   InterPro; IPR004652; tRNA_dU_NifR3.
DR   InterPro; IPR001269; tRNA_hU_synthase.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   Pfam; PF01207; Dus; 1.
DR   PIRSF; PIRSF006621; Dus; 1.
DR   TIGRFAMs; TIGR00737; nifR3_yhdG; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KIP7.
DR   SWISS-2DPAGE; Q3KIP7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02042,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_02042, ECO:0000256|PIRNR:PIRNR006621};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02042};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02042,
KW   ECO:0000256|PIRNR:PIRNR006621, ECO:0000313|EMBL:ABA72359.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_02042};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_02042,
KW   ECO:0000256|PIRNR:PIRNR006621};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   NP_BIND      19     21       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   NP_BIND     203    205       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   NP_BIND     227    228       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   ACT_SITE    103    103       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02042, ECO:0000256|PIRSR:PIRSR006621-
FT                                1}.
FT   BINDING      73     73       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
FT   BINDING     142    142       FMN. {ECO:0000256|HAMAP-Rule:MF_02042}.
SQ   SEQUENCE   336 AA;  36398 MW;  DCC272551565E7A1 CRC64;
     MSAVRIGPYT LQNGLILAPM AGVTDQPFRQ LCKRLGAGLV VSEMVTSDMS LWNTRKSRMR
     MIHEGDPEPR SVQIAGGDAQ MLADAARANV ELGAQIIDIN MGCPAKKVCN KAAGSALLKD
     EALVTEILNA VVAAVDVPVT LKIRTGWDRD NKNGLTVAKI AEQAGITALA VHGRTRADLY
     TGEAEYDTIA AIKQAVSIPV FANGDIVSPE KARYVLDATG ADGLLIGRAA QGRPWIFREI
     EHFLRTGEKL PAPELIEVER ILLEHLAALH AFYGDVMGVR IARKHVGWYL ATLPGAREFR
     AHFNRLDGTE TQCANVREFF AERYKSLTGD GEGVAA
//

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