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P21524

- RIR1_YEAST

UniProt

P21524 - RIR1_YEAST

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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

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
    Complete GO annotation...

    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
    Complete GO annotation...

    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. 60 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.
    InParanoidiP21524.
    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

            10         20         30         40         50
    MYVYKRDGRK EPVQFDKITA RISRLCYGLD PKHIDAVKVT QRIISGVYEG
    60 70 80 90 100
    VTTIELDNLA AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVVED
    110 120 130 140 150
    LYRYVNAATG KPAPMISDDV YNIVMENKDK LNSAIVYDRD FQYSYFGFKT
    160 170 180 190 200
    LERSYLLRIN GQVAERPQHL IMRVALGIHG RDIEAALETY NLMSLKYFTH
    210 220 230 240 250
    ASPTLFNAGT PKPQMSSCFL VAMKEDSIEG IYDTLKECAL ISKTAGGIGL
    260 270 280 290 300
    HIHNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALY
    310 320 330 340 350
    LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEENGTWTL
    360 370 380 390 400
    FSPTSAPGLS DCYGDEFEAL YTRYEKEGRG KTIKAQKLWY SILEAQTETG
    410 420 430 440 450
    TPFVVYKDAC NRKSNQKNLG VIKSSNLCCE IVEYSAPDET AVCNLASVAL
    460 470 480 490 500
    PAFIETSEDG KTSTYNFKKL HEIAKVVTRN LNRVIDRNYY PVEEARKSNM
    510 520 530 540 550
    RHRPIALGVQ GLADTFMLLR LPFDSEEARL LNIQIFETIY HASMEASCEL
    560 570 580 590 600
    AQKDGPYETF QGSPASQGIL QFDMWDQKPY GMWDWDTLRK DIMKHGVRNS
    610 620 630 640 650
    LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV
    660 670 680 690 700
    DLGIWDEGMK QYLITQNGSI QGLPNVPQEL KDLYKTVWEI SQKTIINMAA
    710 720 730 740 750
    DRSVYIDQSH SLNLFLRAPT MGKLTSMHFY GWKKGLKTGM YYLRTQAASA
    760 770 780 790 800
    AIQFTIDQKI ADQATENVAD ISNLKRPSYM PSSASYAASD FVPAAVTANA
    810 820 830 840 850
    TIPSLDSSSE ASREASPAPT GSHSLTKGMA ELNVQESKVE VPEVPAPTKN
    860 870 880
    EEKAAPIVDD EETEFDIYNS KVIACAIDNP EACEMCSG
    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. 60 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.
    InParanoidi P21524.
    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

    « Hide 'large scale' publications
    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 29, 2014
    This is version 148 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