Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00452

- RIR1_ECOLI

UniProt

P00452 - RIR1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP00452.
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

        10         20         30         40         50
MNQNLLVTKR DGSTERINLD KIHRVLDWAA EGLHNVSISQ VELRSHIQFY
60 70 80 90 100
DGIKTSDIHE TIIKAAADLI SRDAPDYQYL AARLAIFHLR KKAYGQFEPP
110 120 130 140 150
ALYDHVVKMV EMGKYDNHLL EDYTEEEFKQ MDTFIDHDRD MTFSYAAVKQ
160 170 180 190 200
LEGKYLVQNR VTGEIYESAQ FLYILVAACL FSNYPRETRL QYVKRFYDAV
210 220 230 240 250
STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT SSAIVKYVSQ
260 270 280 290 300
RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG
310 320 330 340 350
AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG
360 370 380 390 400
EDITLFSPSD VPGLYDAFFA DQEEFERLYT KYEKDDSIRK QRVKAVELFS
410 420 430 440 450
LMMQERASTG RIYIQNVDHC NTHSPFDPAI APVRQSNLCL EIALPTKPLN
460 470 480 490 500
DVNDENGEIA LCTLSAFNLG AINNLDELEE LAILAVRALD ALLDYQDYPI
510 520 530 540 550
PAAKRGAMGR RTLGIGVINF AYYLAKHGKR YSDGSANNLT HKTFEAIQYY
560 570 580 590 600
LLKASNELAK EQGACPWFNE TTYAKGILPI DTYKKDLDTI ANEPLHYDWE
610 620 630 640 650
ALRESIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG YVSIKASKDG
660 670 680 690 700
ILRQVVPDYE HLHDAYELLW EMPGNDGYLQ LVGIMQKFID QSISANTNYD
710 720 730 740 750
PSRFPSGKVP MQQLLKDLLT AYKFGVKTLY YQNTRDGAED AQDDLVPSIQ
760
DDGCESGACK I
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.
InParanoidi P00452.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 160 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