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P21524

- RIR1_YEAST

UniProt

P21524 - RIR1_YEAST

Protein

Ribonucleoside-diphosphate reductase large chain 1

Gene

RNR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.1 Publication

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

    Enzyme regulationi

    Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the R1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site. Inhibited by SML1.1 Publication

    Kineticsi

      Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate1 Publication

      Temperature dependencei

      Optimum temperature is 30 degrees Celsius.1 Publication

      Pathwayi

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Binding sitei5 – 51Allosteric activatorBy similarity
      Binding sitei53 – 531Allosteric activatorBy similarity
      Binding sitei88 – 881Allosteric activatorBy similarity
      Binding sitei202 – 2021Substrate
      Sitei218 – 2181Important for hydrogen atom transferBy similarity
      Sitei226 – 2261Allosteric effector binding, determines substrate specificity
      Binding sitei247 – 2471Substrate; via amide nitrogen
      Sitei256 – 2561Allosteric effector binding, determines substrate specificity
      Active sitei426 – 4261Proton acceptor
      Active sitei428 – 4281Cysteine radical intermediate
      Active sitei430 – 4301Proton acceptor
      Sitei443 – 4431Important for hydrogen atom transferBy similarity
      Sitei741 – 7411Important for electron transferBy similarity
      Sitei742 – 7421Important for electron transferBy similarity
      Sitei883 – 8831Interacts with thioredoxin/glutaredoxinBy similarity
      Sitei886 – 8861Interacts with thioredoxin/glutaredoxinBy similarity

      GO - Molecular functioni

      1. ATP binding Source: UniProtKB-KW
      2. nucleotide binding Source: SGD
      3. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

      GO - Biological processi

      1. deoxyribonucleotide biosynthetic process Source: UniProtKB
      2. DNA replication Source: UniProtKB-UniPathway

      Keywords - Molecular functioni

      Oxidoreductase

      Keywords - Biological processi

      DNA replication

      Keywords - Ligandi

      ATP-binding, Nucleotide-binding

      Enzyme and pathway databases

      BioCyciMetaCyc:YER070W-MONOMER.
      YEAST:YER070W-MONOMER.
      UniPathwayiUPA00326.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Ribonucleoside-diphosphate reductase large chain 1 (EC:1.17.4.1)
      Alternative name(s):
      Ribonucleotide reductase R1 subunit 1
      Ribonucleotide reductase large subunit 1
      Gene namesi
      Name:RNR1
      Synonyms:CRT7, RIR1, SDS12
      Ordered Locus Names:YER070W
      OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
      Taxonomic identifieri559292 [NCBI]
      Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
      ProteomesiUP000002311: Chromosome V

      Organism-specific databases

      CYGDiYER070w.
      SGDiS000000872. RNR1.

      Subcellular locationi

      Cytoplasm 1 Publication

      GO - Cellular componenti

      1. cytoplasm Source: SGD
      2. ribonucleoside-diphosphate reductase complex Source: SGD

      Keywords - Cellular componenti

      Cytoplasm

      Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Mutagenesisi428 – 4281C → A: Completely abolishes reductase activity. 1 Publication

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 888888Ribonucleoside-diphosphate reductase large chain 1PRO_0000187203Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Disulfide bondi218 ↔ 443Redox-active1 Publication
      Modified residuei227 – 2271Phosphoserine1 Publication
      Modified residuei837 – 8371Phosphoserine1 Publication
      Modified residuei887 – 8871Phosphoserine2 Publications

      Keywords - PTMi

      Disulfide bond, Phosphoprotein

      Proteomic databases

      MaxQBiP21524.
      PaxDbiP21524.
      PeptideAtlasiP21524.
      PRIDEiP21524.

      Expressioni

      Inductioni

      Cell cycle-regulated with highest activity in S phase. Moderately induced by DNA-damage.1 Publication

      Gene expression databases

      GenevestigatoriP21524.

      Interactioni

      Subunit structurei

      Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts with the ribonucleotide reductase inhibitor SML1.4 Publications

      Protein-protein interaction databases

      BioGridi36813. 59 interactions.
      DIPiDIP-6299N.
      IntActiP21524. 10 interactions.
      MINTiMINT-680321.
      STRINGi4932.YER070W.

      Structurei

      Secondary structure

      1
      888
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Helixi19 – 235
      Turni31 – 333
      Helixi36 – 416
      Helixi53 – 6614
      Turni67 – 704
      Helixi79 – 8911
      Helixi94 – 1029
      Turni107 – 1104
      Helixi118 – 1269
      Helixi128 – 1325
      Helixi137 – 1426
      Helixi145 – 15410
      Beta strandi158 – 1636
      Helixi167 – 17913
      Helixi183 – 19412
      Beta strandi197 – 2004
      Helixi202 – 2076
      Beta strandi210 – 2123
      Beta strandi218 – 2225
      Helixi228 – 24215
      Turni243 – 2453
      Beta strandi247 – 2515
      Turni263 – 2664
      Helixi272 – 28514
      Turni288 – 2914
      Beta strandi297 – 3015
      Helixi308 – 3114
      Turni312 – 3154
      Beta strandi317 – 3193
      Helixi321 – 3233
      Beta strandi328 – 3347
      Helixi336 – 3438
      Beta strandi347 – 3515
      Turni353 – 3553
      Helixi359 – 3613
      Helixi364 – 37613
      Beta strandi380 – 3845
      Helixi385 – 39915
      Beta strandi403 – 4064
      Helixi407 – 4126
      Turni415 – 4195
      Beta strandi427 – 4293
      Beta strandi441 – 4433
      Beta strandi445 – 4495
      Helixi450 – 4534
      Beta strandi454 – 4563
      Beta strandi458 – 4625
      Beta strandi463 – 4653
      Helixi467 – 48721
      Helixi493 – 50210
      Beta strandi506 – 5105
      Helixi512 – 5198
      Helixi526 – 55429
      Helixi564 – 5674
      Helixi571 – 5744
      Beta strandi581 – 5833
      Helixi585 – 59511
      Helixi611 – 6155
      Beta strandi619 – 6224
      Beta strandi627 – 6293
      Beta strandi634 – 6363
      Beta strandi638 – 6414
      Helixi643 – 6519
      Helixi657 – 6648
      Turni665 – 6684
      Helixi678 – 6836
      Helixi687 – 6893
      Helixi692 – 70312
      Beta strandi714 – 7185
      Helixi721 – 73414
      Beta strandi737 – 7415
      Beta strandi743 – 7453
      Turni748 – 7514
      Helixi760 – 7634
      Helixi764 – 7663
      Turni789 – 7913

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      1ZYZX-ray2.90A/B1-888[»]
      1ZZDX-ray2.60A1-888[»]
      2CVSX-ray2.60A1-888[»]
      2CVTX-ray3.20A1-888[»]
      2CVUX-ray2.90A1-888[»]
      2CVVX-ray2.90A1-888[»]
      2CVWX-ray2.40A1-888[»]
      2CVXX-ray2.20A1-888[»]
      2CVYX-ray2.40A1-888[»]
      2EUDX-ray2.30A1-888[»]
      2ZLFX-ray2.59A1-888[»]
      2ZLGX-ray2.52A1-888[»]
      3K8TX-ray2.10A1-888[»]
      3PAWX-ray6.61A/B/C/D1-888[»]
      3RSRX-ray2.30A1-888[»]
      3S87X-ray2.25A1-888[»]
      3S8AX-ray2.90A1-888[»]
      3S8BX-ray2.80A1-888[»]
      3S8CX-ray2.77A1-888[»]
      3TB9X-ray2.53A1-888[»]
      3TBAX-ray2.80A1-888[»]
      ProteinModelPortaliP21524.
      SMRiP21524. Positions 15-796.
      ModBaseiSearch...
      MobiDBiSearch...

      Miscellaneous databases

      EvolutionaryTraceiP21524.

      Family & Domainsi

      Domains and Repeats

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
      BLAST

      Region

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Regioni11 – 177Allosteric activator bindingBy similarity
      Regioni217 – 2182Substrate binding
      Regioni285 – 2884Allosteric effector binding, determines substrate specificity
      Regioni426 – 4305Substrate binding
      Regioni607 – 6115Substrate binding

      Sequence similaritiesi

      Contains 1 ATP-cone domain.PROSITE-ProRule annotation

      Phylogenomic databases

      eggNOGiCOG0209.
      GeneTreeiENSGT00750000117986.
      HOGENOMiHOG000057035.
      KOiK10807.
      OMAiANGSIQH.
      OrthoDBiEOG7C5MHR.

      Family and domain databases

      InterProiIPR005144. ATP-cone.
      IPR013346. NrdE_NrdA.
      IPR000788. RNR_lg_C.
      IPR013509. RNR_lsu_N.
      IPR008926. RNR_R1-su_N.
      [Graphical view]
      PfamiPF03477. ATP-cone. 1 hit.
      PF02867. Ribonuc_red_lgC. 1 hit.
      PF00317. Ribonuc_red_lgN. 1 hit.
      [Graphical view]
      PRINTSiPR01183. RIBORDTASEM1.
      SUPFAMiSSF48168. SSF48168. 1 hit.
      TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
      PROSITEiPS51161. ATP_CONE. 1 hit.
      PS00089. RIBORED_LARGE. 1 hit.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

      P21524-1 [UniParc]FASTAAdd to Basket

      « Hide

      MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG    50
      VTTIELDNLA AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED 100
      LYRYVNAATG KPAPMISDDV YNIVMENKDK LNSAIVYDRD FQYSYFGFKT 150
      LERSYLLRIN GQVAERPQHL IMRVALGIHG RDIEAALETY NLMSLKYFTH 200
      ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL ISKTAGGIGL 250
      HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY 300
      LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL 350
      FSPTSAPGLS DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG 400
      TPFVVYKDAC NRKSNQKNLG VIKSSNLCCE IVEYSAPDET AVCNLASVAL 450
      PAFIETSEDG KTSTYNFKKL HEIAKVVTRN LNRVIDRNYY PVEEARKSNM 500
      RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY HASMEASCEL 550
      AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS 600
      LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV 650
      DLGIWDEGMK QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA 700
      DRSVYIDQSH SLNLFLRAPT MGKLTSMHFY GWKKGLKTGM YYLRTQAASA 750
      AIQFTIDQKI ADQATENVAD ISNLKRPSYM PSSASYAASD FVPAAVTANA 800
      TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE VPEVPAPTKN 850
      EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG 888
      Length:888
      Mass (Da):99,561
      Last modified:February 1, 1995 - v2
      Checksum:i56BE1B077916E419
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti329 – 3291F → L in CAA49151. (PubMed:8121398)Curated
      Sequence conflicti587 – 5893TLR → NLK in CAA49150. (PubMed:8121398)Curated
      Sequence conflicti666 – 6661Q → E no nucleotide entry (PubMed:2199320)Curated
      Sequence conflicti679 – 6791E → Q no nucleotide entry (PubMed:2199320)Curated

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      U18813 Genomic DNA. Translation: AAB64606.1.
      X69216 Genomic DNA. Translation: CAA49150.1.
      X69217 Genomic DNA. Translation: CAA49151.1.
      BK006939 Genomic DNA. Translation: DAA07729.1.
      PIRiS50573.
      RefSeqiNP_010993.1. NM_001178961.1.

      Genome annotation databases

      EnsemblFungiiYER070W; YER070W; YER070W.
      GeneIDi856801.
      KEGGisce:YER070W.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      U18813 Genomic DNA. Translation: AAB64606.1 .
      X69216 Genomic DNA. Translation: CAA49150.1 .
      X69217 Genomic DNA. Translation: CAA49151.1 .
      BK006939 Genomic DNA. Translation: DAA07729.1 .
      PIRi S50573.
      RefSeqi NP_010993.1. NM_001178961.1.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      1ZYZ X-ray 2.90 A/B 1-888 [» ]
      1ZZD X-ray 2.60 A 1-888 [» ]
      2CVS X-ray 2.60 A 1-888 [» ]
      2CVT X-ray 3.20 A 1-888 [» ]
      2CVU X-ray 2.90 A 1-888 [» ]
      2CVV X-ray 2.90 A 1-888 [» ]
      2CVW X-ray 2.40 A 1-888 [» ]
      2CVX X-ray 2.20 A 1-888 [» ]
      2CVY X-ray 2.40 A 1-888 [» ]
      2EUD X-ray 2.30 A 1-888 [» ]
      2ZLF X-ray 2.59 A 1-888 [» ]
      2ZLG X-ray 2.52 A 1-888 [» ]
      3K8T X-ray 2.10 A 1-888 [» ]
      3PAW X-ray 6.61 A/B/C/D 1-888 [» ]
      3RSR X-ray 2.30 A 1-888 [» ]
      3S87 X-ray 2.25 A 1-888 [» ]
      3S8A X-ray 2.90 A 1-888 [» ]
      3S8B X-ray 2.80 A 1-888 [» ]
      3S8C X-ray 2.77 A 1-888 [» ]
      3TB9 X-ray 2.53 A 1-888 [» ]
      3TBA X-ray 2.80 A 1-888 [» ]
      ProteinModelPortali P21524.
      SMRi P21524. Positions 15-796.
      ModBasei Search...
      MobiDBi Search...

      Protein-protein interaction databases

      BioGridi 36813. 59 interactions.
      DIPi DIP-6299N.
      IntActi P21524. 10 interactions.
      MINTi MINT-680321.
      STRINGi 4932.YER070W.

      Proteomic databases

      MaxQBi P21524.
      PaxDbi P21524.
      PeptideAtlasi P21524.
      PRIDEi P21524.

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      EnsemblFungii YER070W ; YER070W ; YER070W .
      GeneIDi 856801.
      KEGGi sce:YER070W.

      Organism-specific databases

      CYGDi YER070w.
      SGDi S000000872. RNR1.

      Phylogenomic databases

      eggNOGi COG0209.
      GeneTreei ENSGT00750000117986.
      HOGENOMi HOG000057035.
      KOi K10807.
      OMAi ANGSIQH.
      OrthoDBi EOG7C5MHR.

      Enzyme and pathway databases

      UniPathwayi UPA00326 .
      BioCyci MetaCyc:YER070W-MONOMER.
      YEAST:YER070W-MONOMER.

      Miscellaneous databases

      EvolutionaryTracei P21524.
      NextBioi 983047.

      Gene expression databases

      Genevestigatori P21524.

      Family and domain databases

      InterProi IPR005144. ATP-cone.
      IPR013346. NrdE_NrdA.
      IPR000788. RNR_lg_C.
      IPR013509. RNR_lsu_N.
      IPR008926. RNR_R1-su_N.
      [Graphical view ]
      Pfami PF03477. ATP-cone. 1 hit.
      PF02867. Ribonuc_red_lgC. 1 hit.
      PF00317. Ribonuc_red_lgN. 1 hit.
      [Graphical view ]
      PRINTSi PR01183. RIBORDTASEM1.
      SUPFAMi SSF48168. SSF48168. 1 hit.
      TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
      PROSITEi PS51161. ATP_CONE. 1 hit.
      PS00089. RIBORED_LARGE. 1 hit.
      [Graphical view ]
      ProtoNeti Search...

      Publicationsi

      1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
        Strain: ATCC 204508 / S288c.
      2. Cited for: GENOME REANNOTATION.
        Strain: ATCC 204508 / S288c.
      3. "Two genes differentially regulated in the cell cycle and by DNA-damaging agents encode alternative regulatory subunits of ribonucleotide reductase."
        Elledge S.J., Davis R.W.
        Genes Dev. 4:740-751(1990) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100 AND 653-682, INDUCTION.
      4. "Use of synthetic lethal mutants to clone and characterize a novel CTP synthetase gene in Saccharomyces cerevisiae."
        Ozier-Kalogeropoulos O., Adeline M.-T., Yang W.-L., Carman G.M., Lacroute F.
        Mol. Gen. Genet. 242:431-439(1994) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-384 AND 546-590.
      5. "Yeast Sml1, a protein inhibitor of ribonucleotide reductase."
        Chabes A., Domkin V., Thelander L.
        J. Biol. Chem. 274:36679-36683(1999) [PubMed] [Europe PMC] [Abstract]
        Cited for: INTERACTION WITH SML1, ENZYME REGULATION.
      6. "Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit."
        Chabes A., Domkin V., Larsson G., Liu A., Graeslund A., Wijmenga S., Thelander L.
        Proc. Natl. Acad. Sci. U.S.A. 97:2474-2479(2000) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      7. "Yeast DNA damage-inducible Rnr3 has a very low catalytic activity strongly stimulated after the formation of a cross-talking Rnr1/Rnr3 complex."
        Domkin V., Thelander L., Chabes A.
        J. Biol. Chem. 277:18574-18578(2002) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, MUTAGENESIS OF CYS-428.
      8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
      9. "Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways."
        Yao R., Zhang Z., An X., Bucci B., Perlstein D.L., Stubbe J., Huang M.
        Proc. Natl. Acad. Sci. U.S.A. 100:6628-6633(2003) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBCELLULAR LOCATION.
      10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
        Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
        Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-837 AND SER-887, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
        Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
        Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
        Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
        Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
        Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      13. "Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation."
        Xu H., Faber C., Uchiki T., Fairman J.W., Racca J., Dealwis C.
        Proc. Natl. Acad. Sci. U.S.A. 103:4022-4027(2006) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH CDP; UDP; TTP; GDP; GTP; ADP AND AMPPNP, DISULFIDE BOND.
      14. "Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly."
        Xu H., Faber C., Uchiki T., Racca J., Dealwis C.
        Proc. Natl. Acad. Sci. U.S.A. 103:4028-4033(2006) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH GEMCITABINE DIPHOSPHATE AND R2 PEPTIDES, SUBUNIT.
      15. "The structural basis for peptidomimetic inhibition of eukaryotic ribonucleotide reductase: a conformationally flexible pharmacophore."
        Xu H., Fairman J.W., Wijerathna S.R., Kreischer N.R., LaMacchia J., Helmbrecht E., Cooperman B.S., Dealwis C.
        J. Med. Chem. 51:4653-4659(2008) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH PEPTIDE INHIBITORS, SUBUNIT.

      Entry informationi

      Entry nameiRIR1_YEAST
      AccessioniPrimary (citable) accession number: P21524
      Secondary accession number(s): D3DLX5
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: May 1, 1991
      Last sequence update: February 1, 1995
      Last modified: October 1, 2014
      This is version 147 of the entry and version 2 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programFungal Protein Annotation Program

      Miscellaneousi

      Miscellaneous

      Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2 By similarity.By similarity
      Present with 293000 molecules/cell in log phase SD medium.1 Publication

      Keywords - Technical termi

      3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

      Documents

      1. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      2. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      3. SIMILARITY comments
        Index of protein domains and families
      4. Yeast
        Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
      5. Yeast chromosome V
        Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

      External Data

      Dasty 3