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P00452

- RIR1_ECOLI

UniProt

P00452 - RIR1_ECOLI

Protein

Ribonucleoside-diphosphate reductase 1 subunit alpha

Gene

nrdA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines.

    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 alpha 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. In vitro, its activity is increased by dithiothreitol (DTT) or thioredoxins (non-specific).2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Allosteric activator
    Binding sitei55 – 551Allosteric activator
    Binding sitei91 – 911Allosteric activator
    Binding sitei209 – 2091Substrate
    Sitei225 – 2251Important for hydrogen atom transfer
    Sitei232 – 2321Allosteric effector binding
    Binding sitei253 – 2531Substrate; via amide nitrogenBy similarity
    Sitei262 – 2621Allosteric effector binding
    Active sitei437 – 4371Proton acceptor
    Active sitei439 – 4391Cysteine radical intermediate
    Active sitei441 – 4411Proton acceptor
    Sitei462 – 4621Important for hydrogen atom transfer
    Sitei730 – 7301Important for electron transfer
    Sitei731 – 7311Important for electron transfer
    Sitei754 – 7541Interacts with thioredoxin/glutaredoxin
    Sitei759 – 7591Interacts with thioredoxin/glutaredoxin

    GO - Molecular functioni

    1. ATP binding Source: EcoliWiki
    2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: EcoCyc

    GO - Biological processi

    1. deoxyribonucleotide biosynthetic process Source: EcoliWiki
    2. DNA replication Source: UniProtKB-UniPathway
    3. nucleobase-containing small molecule interconversion Source: EcoliWiki

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:NRDA-MONOMER.
    ECOL316407:JW2228-MONOMER.
    MetaCyc:NRDA-MONOMER.
    SABIO-RKP00452.
    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase 1 subunit alpha (EC:1.17.4.1)
    Alternative name(s):
    Protein B1
    Ribonucleoside-diphosphate reductase 1 R1 subunit
    Ribonucleotide reductase 1
    Gene namesi
    Name:nrdA
    Synonyms:dnaF
    Ordered Locus Names:b2234, JW2228
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10660. nrdA.

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: EcoliWiki

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi441 – 4411E → A or Q: Loss of activity. 1 Publication
    Mutagenesisi441 – 4411E → D: Decrease in activity. 1 Publication
    Mutagenesisi730 – 7301Y → F: Loss of activity. 1 Publication
    Mutagenesisi731 – 7311Y → F: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 761761Ribonucleoside-diphosphate reductase 1 subunit alphaPRO_0000030596Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi225 ↔ 462Redox-active2 Publications
    Modified residuei283 – 2831N6-acetyllysine1 Publication

    Post-translational modificationi

    Binding of the substrate occurs primarily when the active-site cysteines are reduced.

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    PaxDbiP00452.
    PRIDEiP00452.

    Expressioni

    Gene expression databases

    GenevestigatoriP00452.

    Interactioni

    Subunit structurei

    Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 protein is a dimer of alpha subunits. A radical transfer pathway occurs between 'Tyr-122' of R2 and R1.2 Publications

    Protein-protein interaction databases

    DIPiDIP-584N.
    IntActiP00452. 9 interactions.
    MINTiMINT-1233906.
    STRINGi511145.b2234.

    Structurei

    Secondary structure

    1
    761
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi10 – 123
    Beta strandi14 – 163
    Helixi19 – 3012
    Helixi38 – 469
    Helixi55 – 6814
    Beta strandi72 – 743
    Helixi77 – 9418
    Beta strandi95 – 984
    Helixi102 – 11110
    Helixi118 – 1225
    Helixi125 – 13410
    Helixi137 – 1426
    Helixi145 – 15410
    Turni160 – 1623
    Helixi169 – 18012
    Turni181 – 1833
    Turni186 – 1883
    Helixi189 – 20113
    Beta strandi204 – 2063
    Helixi209 – 2146
    Beta strandi225 – 2295
    Helixi234 – 24815
    Turni249 – 2513
    Beta strandi253 – 2575
    Beta strandi268 – 2714
    Helixi274 – 2763
    Helixi278 – 28912
    Turni290 – 2923
    Beta strandi296 – 2994
    Beta strandi301 – 3077
    Helixi313 – 3175
    Turni318 – 3203
    Beta strandi322 – 3243
    Helixi326 – 3283
    Beta strandi333 – 3397
    Helixi341 – 3499
    Beta strandi352 – 3565
    Helixi358 – 3603
    Helixi364 – 3707
    Helixi372 – 38413
    Beta strandi386 – 3883
    Beta strandi391 – 3944
    Helixi395 – 40915
    Beta strandi412 – 4165
    Helixi419 – 4224
    Beta strandi423 – 4264
    Turni428 – 4303
    Beta strandi463 – 4686
    Turni469 – 4713
    Helixi475 – 4773
    Helixi478 – 49518
    Helixi501 – 51010
    Beta strandi513 – 5186
    Helixi520 – 5267
    Beta strandi531 – 5344
    Helixi537 – 56226
    Helixi568 – 5703
    Helixi573 – 5753
    Helixi579 – 5824
    Helixi585 – 5895
    Helixi599 – 60911
    Beta strandi612 – 6143
    Helixi624 – 6285
    Beta strandi639 – 6457
    Beta strandi648 – 6503
    Beta strandi652 – 6554
    Helixi659 – 6624
    Turni663 – 6653
    Helixi669 – 6713
    Beta strandi672 – 6754
    Helixi676 – 68611
    Beta strandi697 – 6993
    Helixi701 – 7033
    Helixi705 – 7073
    Helixi711 – 72313
    Beta strandi732 – 7343
    Helixi738 – 7414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QFNNMR-B737-761[»]
    1R1RX-ray2.90A/B/C1-761[»]
    1RLRX-ray2.50A1-761[»]
    2R1RX-ray3.00A/B/C1-761[»]
    2X0XX-ray2.30A/B/C1-761[»]
    2XAKX-ray2.80A/B/C1-761[»]
    2XAPX-ray2.10A/B/C1-761[»]
    2XAVX-ray2.80A/B/C1-761[»]
    2XAWX-ray3.10A/B/C1-761[»]
    2XAXX-ray2.75A/B/C1-761[»]
    2XAYX-ray2.65A/B/C1-761[»]
    2XAZX-ray2.60A/B/C1-761[»]
    2XO4X-ray2.50A/B/C1-761[»]
    2XO5X-ray2.70A/B/C1-761[»]
    3R1RX-ray3.00A/B/C1-761[»]
    3UUSX-ray5.65A/B/C/D1-761[»]
    4ERMX-ray3.95A/B/C/D1-761[»]
    4ERPX-ray4.45A/B/C/D1-761[»]
    4R1RX-ray3.20A/B/C1-761[»]
    5R1RX-ray3.10A/B/C1-761[»]
    6R1RX-ray3.10A/B/C1-761[»]
    7R1RX-ray3.10A/B/C1-761[»]
    ProteinModelPortaliP00452.
    SMRiP00452. Positions 4-737.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00452.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9591ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 217Allosteric activator binding
    Regioni224 – 2252Substrate bindingBy similarity
    Regioni437 – 4415Substrate bindingBy similarity
    Regioni621 – 6255Substrate binding

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    HOGENOMiHOG000278076.
    KOiK00525.
    OMAiLLWQMPS.
    OrthoDBiEOG6J48HC.
    PhylomeDBiP00452.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Alpha (identifier: P00452-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNQNLLVTKR DGSTERINLD KIHRVLDWAA EGLHNVSISQ VELRSHIQFY    50
    DGIKTSDIHE TIIKAAADLI SRDAPDYQYL AARLAIFHLR KKAYGQFEPP 100
    ALYDHVVKMV EMGKYDNHLL EDYTEEEFKQ MDTFIDHDRD MTFSYAAVKQ 150
    LEGKYLVQNR VTGEIYESAQ FLYILVAACL FSNYPRETRL QYVKRFYDAV 200
    STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT SSAIVKYVSQ 250
    RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG 300
    AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG 350
    EDITLFSPSD VPGLYDAFFA DQEEFERLYT KYEKDDSIRK QRVKAVELFS 400
    LMMQERASTG RIYIQNVDHC NTHSPFDPAI APVRQSNLCL EIALPTKPLN 450
    DVNDENGEIA LCTLSAFNLG AINNLDELEE LAILAVRALD ALLDYQDYPI 500
    PAAKRGAMGR RTLGIGVINF AYYLAKHGKR YSDGSANNLT HKTFEAIQYY 550
    LLKASNELAK EQGACPWFNE TTYAKGILPI DTYKKDLDTI ANEPLHYDWE 600
    ALRESIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG YVSIKASKDG 650
    ILRQVVPDYE HLHDAYELLW EMPGNDGYLQ LVGIMQKFID QSISANTNYD 700
    PSRFPSGKVP MQQLLKDLLT AYKFGVKTLY YQNTRDGAED AQDDLVPSIQ 750
    DDGCESGACK I 761
    Length:761
    Mass (Da):85,775
    Last modified:November 1, 1997 - v2
    Checksum:i7E034F154567C3FC
    GO
    Isoform Alpha' (identifier: P00452-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: Missing.
         26-26: L → M

    Show »
    Length:736
    Mass (Da):82,860
    Checksum:i498ADEDC2154C084
    GO

    Sequence cautioni

    The sequence AAA24223.1 differs from that shown. Reason:

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 22Missing in 15% of the chains.
    Natural varianti1 – 11Missing in 30% of the chains.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525Missing in isoform Alpha'. CuratedVSP_018871Add
    BLAST
    Alternative sequencei26 – 261L → M in isoform Alpha'. CuratedVSP_018872

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02672 Genomic DNA. Translation: AAA24223.1. Sequence problems.
    X06999 Genomic DNA. Translation: CAA30056.2.
    U00096 Genomic DNA. Translation: AAC75294.1.
    AP009048 Genomic DNA. Translation: BAA16053.1.
    PIRiH64993. RDEC1R.
    RefSeqiNP_416737.1. NC_000913.3.
    YP_490473.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75294; AAC75294; b2234.
    BAA16053; BAA16053; BAA16053.
    GeneIDi12933136.
    946612.
    KEGGiecj:Y75_p2196.
    eco:b2234.
    PATRICi32119827. VBIEscCol129921_2323.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02672 Genomic DNA. Translation: AAA24223.1 . Sequence problems.
    X06999 Genomic DNA. Translation: CAA30056.2 .
    U00096 Genomic DNA. Translation: AAC75294.1 .
    AP009048 Genomic DNA. Translation: BAA16053.1 .
    PIRi H64993. RDEC1R.
    RefSeqi NP_416737.1. NC_000913.3.
    YP_490473.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QFN NMR - B 737-761 [» ]
    1R1R X-ray 2.90 A/B/C 1-761 [» ]
    1RLR X-ray 2.50 A 1-761 [» ]
    2R1R X-ray 3.00 A/B/C 1-761 [» ]
    2X0X X-ray 2.30 A/B/C 1-761 [» ]
    2XAK X-ray 2.80 A/B/C 1-761 [» ]
    2XAP X-ray 2.10 A/B/C 1-761 [» ]
    2XAV X-ray 2.80 A/B/C 1-761 [» ]
    2XAW X-ray 3.10 A/B/C 1-761 [» ]
    2XAX X-ray 2.75 A/B/C 1-761 [» ]
    2XAY X-ray 2.65 A/B/C 1-761 [» ]
    2XAZ X-ray 2.60 A/B/C 1-761 [» ]
    2XO4 X-ray 2.50 A/B/C 1-761 [» ]
    2XO5 X-ray 2.70 A/B/C 1-761 [» ]
    3R1R X-ray 3.00 A/B/C 1-761 [» ]
    3UUS X-ray 5.65 A/B/C/D 1-761 [» ]
    4ERM X-ray 3.95 A/B/C/D 1-761 [» ]
    4ERP X-ray 4.45 A/B/C/D 1-761 [» ]
    4R1R X-ray 3.20 A/B/C 1-761 [» ]
    5R1R X-ray 3.10 A/B/C 1-761 [» ]
    6R1R X-ray 3.10 A/B/C 1-761 [» ]
    7R1R X-ray 3.10 A/B/C 1-761 [» ]
    ProteinModelPortali P00452.
    SMRi P00452. Positions 4-737.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-584N.
    IntActi P00452. 9 interactions.
    MINTi MINT-1233906.
    STRINGi 511145.b2234.

    Proteomic databases

    PaxDbi P00452.
    PRIDEi P00452.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75294 ; AAC75294 ; b2234 .
    BAA16053 ; BAA16053 ; BAA16053 .
    GeneIDi 12933136.
    946612.
    KEGGi ecj:Y75_p2196.
    eco:b2234.
    PATRICi 32119827. VBIEscCol129921_2323.

    Organism-specific databases

    EchoBASEi EB0654.
    EcoGenei EG10660. nrdA.

    Phylogenomic databases

    eggNOGi COG0209.
    HOGENOMi HOG000278076.
    KOi K00525.
    OMAi LLWQMPS.
    OrthoDBi EOG6J48HC.
    PhylomeDBi P00452.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci EcoCyc:NRDA-MONOMER.
    ECOL316407:JW2228-MONOMER.
    MetaCyc:NRDA-MONOMER.
    SABIO-RK P00452.

    Miscellaneous databases

    EvolutionaryTracei P00452.
    PROi P00452.

    Gene expression databases

    Genevestigatori P00452.

    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. "Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon."
      Carlson J., Fuchs J.A., Messing J.
      Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction."
      Nilsson O., Aaberg A., Lundqvist T., Sjoeberg B.-M.
      Nucleic Acids Res. 16:4174-4174(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. Sjoeberg B.-M.
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 526-527.
    4. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene."
      Sjoeberg B.-M., Eriksson S., Joernvall H., Carlquist M., Eklund H.
      Eur. J. Biochem. 150:423-427(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    8. "Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli."
      Aaberg A., Hahne S., Karlsson M., Larsson A., Ormoe M., Aahgren A., Sjoeberg B.-M.
      J. Biol. Chem. 264:12249-12252(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES.
    9. "Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase."
      Ekberg M., Sahlin M., Eriksson M., Sjoberg B.M.
      J. Biol. Chem. 271:20655-20659(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES, MUTAGENESIS OF TYR-730 AND TYR-731.
    10. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    11. "Structure of ribonucleotide reductase protein R1."
      Uhlin U., Eklund H.
      Nature 370:533-539(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    12. "A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase."
      Persson A.L., Eriksson M., Katterle B., Potsch S., Sahlin M., Sjoberg B.M.
      J. Biol. Chem. 272:31533-31541(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF MUTANTS ALA-441; ASP-441 AND GLN-441, DISULFIDE BOND, SUBUNIT, ACTIVE SITE, ENZYME REGULATION, ENZYME MECHANISM, MUTAGENESIS OF GLU-441.
    13. "Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding."
      Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K., Sjoeberg B.-M., Eklund H.
      Structure 5:1077-1092(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH ATP; GDP AND TTP, DISULFIDE BOND, SUBUNIT, ENZYME REGULATION.
    14. "Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction."
      Berardi M.J., Bushweller J.H.
      J. Mol. Biol. 292:151-161(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 737-761, BINDING SITES.

    Entry informationi

    Entry nameiRIR1_ECOLI
    AccessioniPrimary (citable) accession number: P00452
    Secondary accession number(s): P78088, P78177
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    E.coli produces two separate class I enzymes. This one is the functional enzyme during growth.
    Two distinct regulatory sites have been defined: one controls substrate specificity and the other regulates the overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3