(data stored in SCRATCH zone)

SWISSPROT: DUS1_BACSU

ID   DUS1_BACSU              Reviewed;         333 AA.
AC   P37567;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Probable tRNA-dihydrouridine synthase 1;
DE            EC=1.3.1.-;
GN   Name=dus1; Synonyms=yacF; OrderedLocusNames=BSU00810;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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:0000250|UniProtKB:P33371}.
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:0000250|UniProtKB:P33371};
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:0000250|UniProtKB:P33371};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P33371};
CC   -!- SIMILARITY: Belongs to the Dus family. {ECO:0000305}.
DR   EMBL; D26185; BAA05315.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11857.1; -; Genomic_DNA.
DR   PIR; S66110; S66110.
DR   RefSeq; NP_387962.1; NC_000964.3.
DR   RefSeq; WP_003243741.1; NZ_JNCM01000028.1.
DR   SMR; P37567; -.
DR   STRING; 224308.BSU00810; -.
DR   PaxDb; P37567; -.
DR   PRIDE; P37567; -.
DR   EnsemblBacteria; CAB11857; CAB11857; BSU00810.
DR   GeneID; 936924; -.
DR   KEGG; bsu:BSU00810; -.
DR   PATRIC; fig|224308.179.peg.81; -.
DR   eggNOG; ENOG4105CEH; Bacteria.
DR   eggNOG; COG0042; LUCA.
DR   HOGENOM; HOG000217853; -.
DR   InParanoid; P37567; -.
DR   OMA; RPWLFAD; -.
DR   PhylomeDB; P37567; -.
DR   BioCyc; BSUB:BSU00810-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 1.10.1200.80; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
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; P37567.
DR   SWISS-2DPAGE; P37567.
KW   Flavoprotein; FMN; NADP; Oxidoreductase; Reference proteome; RNA-binding;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..333
FT                   /note="Probable tRNA-dihydrouridine synthase 1"
FT                   /id="PRO_0000162132"
FT   NP_BIND         17..19
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   NP_BIND         202..204
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   NP_BIND         226..227
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   ACT_SITE        102
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT   BINDING         71
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
FT   BINDING         141
FT                   /note="FMN"
FT                   /evidence="ECO:0000250|UniProtKB:P33371"
SQ   SEQUENCE   333 AA;  37066 MW;  73CC58A422008EFA CRC64;
     MFKIGDIQLK NRVVLAPMAG VCNSAFRLTV KEFGAGLVCA EMVSDKAILY NNARTMGMLY
     IDEREKPLSL QIFGGKKETL VEAAKFVDQN TTADIIDINM GCPVPKITKC DAGAKWLLDP
     DKIYEMVSAV VDAVNKPVTV KMRMGWDEDH IFAVKNAQAV ERAGGKAVAL HGRTRVQMYE
     GTANWDIIKE VKQSVSIPVI GNGDVKTPQD AKRMLDETGV DGVMIGRAAL GNPWMIYRTV
     QYLETGKLKE EPQVREKMAV CKLHLDRLID LKGENVAVRE MRKHAAWYLK GVKGNANVRN
     EINHCETREE FVQLLDAFTV EVEAKELQNA KVG
//

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