Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Anaerobic ribonucleoside-triphosphate reductase (EC 1.1.98.6) (Class III ribonucleoside-triphosphate reductase)

 NRDD_BPT4               Reviewed;         605 AA.
P07071; P07073; Q38428; Q9T0V5;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 4.
22-NOV-2017, entry version 123.
RecName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000305};
EC=1.1.98.6 {ECO:0000269|PubMed:8702830};
AltName: Full=Class III ribonucleoside-triphosphate reductase {ECO:0000305};
Name=nrdD {ECO:0000303|PubMed:8051113};
Synonyms=49.1, 55.11/55.13, SUNY;
Enterobacteria phage T4 (Bacteriophage T4).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Tevenvirinae; T4virus.
NCBI_TaxID=10665;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C;
PubMed=3575111; DOI=10.1093/nar/15.8.3632;
Tomaschewski J., Rueger W.;
"Nucleotide sequence and primary structures of gene products coded for
by the T4 genome between map positions 48.266 kb and 39.166 kb.";
Nucleic Acids Res. 15:3632-3633(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12626685; DOI=10.1128/MMBR.67.1.86-156.2003;
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
PubMed=2974005;
Barth K.A., Powell D., Trupin M., Mosig G.;
"Regulation of two nested proteins from gene 49 (recombination
endonuclease VII) and of a lambda RexA-like protein of bacteriophage
T4.";
Genetics 120:329-343(1988).
[4]
IDENTIFICATION.
PubMed=1938898; DOI=10.1128/jb.173.21.6980-6985.1991;
Zeh A., Shub D.A.;
"The product of the split sunY gene of bacteriophage T4 is a processed
protein.";
J. Bacteriol. 173:6980-6985(1991).
[5]
POSSIBLE FUNCTION.
PubMed=8421692; DOI=10.1073/pnas.90.2.577;
Sun X., Harder J., Krook M., Joernvall H., Sjoeberg B.-M.,
Reichard P.;
"A possible glycine radical in anaerobic ribonucleotide reductase from
Escherichia coli: nucleotide sequence of the cloned nrdD gene.";
Proc. Natl. Acad. Sci. U.S.A. 90:577-581(1993).
[6]
FUNCTION AS AN ANAEROBIC RIBONUCLEOTIDE REDUCTASE.
PubMed=8051113;
Young P., Oehman M., Xu M.Q., Shub D.A., Sjoeberg B.-M.;
"Intron-containing T4 bacteriophage gene sunY encodes an anaerobic
ribonucleotide reductase.";
J. Biol. Chem. 269:20229-20232(1994).
[7]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, INTERACTION
WITH NRDG, GLYCYL RADICAL AT GLY-580, AND MUTAGENESIS OF GLY-580.
PubMed=8702830; DOI=10.1074/jbc.271.34.20770;
Young P., Andersson J., Sahlin M., Sjoeberg B.-M.;
"Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable
glycyl radical at position 580.";
J. Biol. Chem. 271:20770-20775(1996).
[8]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF MUTANT ALA-580.
PubMed=10066165; DOI=10.1126/science.283.5407.1499;
Logan D.T., Andersson J., Sjoeberg B.-M., Nordlund P.;
"A glycyl radical site in the crystal structure of a class III
ribonucleotide reductase.";
Science 283:1499-1504(1999).
[9] {ECO:0000244|PDB:1H78, ECO:0000244|PDB:1H79, ECO:0000244|PDB:1H7A, ECO:0000244|PDB:1H7B}
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEXES WITH DCTP; DTTP;
DATP AND IRON.
PubMed=11587648; DOI=10.1016/S0969-2126(01)00627-X;
Larsson K.M., Andersson J., Sjoberg B.M., Nordlund P., Logan D.T.;
"Structural basis for allosteric substrate specificity regulation in
anaerobic ribonucleotide reductases.";
Structure 9:739-750(2001).
[10] {ECO:0000244|PDB:1HK8}
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH DGTP AND ZINC,
AND ZINC-BINDING.
PubMed=12655046; DOI=10.1073/pnas.0736456100;
Logan D.T., Mulliez E., Larsson K.-M., Bodevin S., Atta M.,
Garnaud P.E., Sjoeberg B.-M., Fontecave M.;
"A metal-binding site in the catalytic subunit of anaerobic
ribonucleotide reductase.";
Proc. Natl. Acad. Sci. U.S.A. 100:3826-3831(2003).
-!- FUNCTION: Catalyzes the conversion of ribonucleotides into
deoxyribonucleotides, which are required for DNA synthesis and
repair. {ECO:0000269|PubMed:8051113, ECO:0000269|PubMed:8702830}.
-!- CATALYTIC ACTIVITY: Ribonucleoside 5'-triphosphate + formate = 2'-
deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O.
{ECO:0000269|PubMed:8702830}.
-!- ENZYME REGULATION: Activated under anaerobic conditions by NrdG, a
tightly associated activase. Activation involves the formation of
a glycyl radical at Gly-580. {ECO:0000269|PubMed:8702830}.
-!- SUBUNIT: Homodimer. Forms a tetramer composed of two NrdD and two
NrdG subunits. {ECO:0000269|PubMed:8702830}.
-!- SIMILARITY: Belongs to the anaerobic ribonucleoside-triphosphate
reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00122; CAA68308.1; -; Genomic_DNA.
EMBL; Y00122; CAA68310.1; ALT_SEQ; Genomic_DNA.
EMBL; AF158101; AAD42633.1; -; Genomic_DNA.
EMBL; X12629; CAA31150.1; -; Genomic_DNA.
PIR; E29284; Z6BPT9.
PIR; S01907; Z4BPT9.
RefSeq; NP_049690.1; NC_000866.4.
PDB; 1H78; X-ray; 2.50 A; A=1-605.
PDB; 1H79; X-ray; 2.90 A; A=1-605.
PDB; 1H7A; X-ray; 2.75 A; A=1-605.
PDB; 1H7B; X-ray; 2.45 A; A=1-605.
PDB; 1HK8; X-ray; 2.45 A; A=1-605.
PDBsum; 1H78; -.
PDBsum; 1H79; -.
PDBsum; 1H7A; -.
PDBsum; 1H7B; -.
PDBsum; 1HK8; -.
ProteinModelPortal; P07071; -.
SMR; P07071; -.
DrugBank; DB03222; 2'-Deoxyadenosine 5'-Triphosphate.
DrugBank; DB03258; 2'-Deoxycytidine-5'-Triphosphate.
DrugBank; DB02181; 2'-Deoxyguanosine-5'-Triphosphate.
DrugBank; DB02452; Thymidine-5'-Triphosphate.
GeneID; 1258655; -.
KEGG; vg:1258655; -.
OrthoDB; VOG0900003Y; -.
EvolutionaryTrace; P07071; -.
PRO; PR:P07071; -.
Proteomes; UP000009087; Genome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IEA:InterPro.
CDD; cd01675; RNR_III; 1.
InterPro; IPR019777; Form_AcTrfase_GR_CS.
InterPro; IPR001150; Gly_radical.
InterPro; IPR012833; NrdD.
Pfam; PF13597; NRDD; 1.
TIGRFAMs; TIGR02487; NrdD; 1.
PROSITE; PS00850; GLY_RADICAL_1; 1.
PROSITE; PS51149; GLY_RADICAL_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Metal-binding; Organic radical;
Oxidoreductase; Reference proteome; Zinc.
CHAIN 1 605 Anaerobic ribonucleoside-triphosphate
reductase.
/FTId=PRO_0000166686.
DOMAIN 482 605 Glycine radical. {ECO:0000255|PROSITE-
ProRule:PRU00493}.
REGION 64 66 Substrate 1 binding.
{ECO:0000269|PubMed:11587648,
ECO:0000269|PubMed:12655046}.
REGION 100 103 Substrate 2 binding.
{ECO:0000269|PubMed:11587648,
ECO:0000269|PubMed:12655046}.
REGION 444 448 Substrate 1 binding.
{ECO:0000269|PubMed:11587648,
ECO:0000269|PubMed:12655046}.
METAL 543 543 Zinc. {ECO:0000269|PubMed:12655046,
ECO:0000305|PubMed:11587648}.
METAL 546 546 Zinc. {ECO:0000269|PubMed:12655046,
ECO:0000305|PubMed:11587648}.
METAL 561 561 Zinc. {ECO:0000269|PubMed:12655046,
ECO:0000305|PubMed:11587648}.
METAL 564 564 Zinc. {ECO:0000269|PubMed:12655046,
ECO:0000305|PubMed:11587648}.
BINDING 114 114 Substrate 2.
{ECO:0000269|PubMed:11587648}.
BINDING 146 146 Substrate 2.
{ECO:0000269|PubMed:11587648,
ECO:0000269|PubMed:12655046}.
MOD_RES 580 580 Glycine radical.
{ECO:0000269|PubMed:8702830}.
MUTAGEN 580 580 G->A: Lacks both glycyl radical and
activity. Does not affect interaction
with NrdG. {ECO:0000269|PubMed:8702830}.
HELIX 30 47 {ECO:0000244|PDB:1H7B}.
HELIX 52 59 {ECO:0000244|PDB:1H7B}.
STRAND 62 65 {ECO:0000244|PDB:1H7B}.
TURN 66 73 {ECO:0000244|PDB:1H7B}.
HELIX 84 89 {ECO:0000244|PDB:1H7B}.
STRAND 92 94 {ECO:0000244|PDB:1H7B}.
STRAND 97 99 {ECO:0000244|PDB:1H7B}.
HELIX 105 120 {ECO:0000244|PDB:1H7B}.
STRAND 123 125 {ECO:0000244|PDB:1H7B}.
STRAND 127 129 {ECO:0000244|PDB:1H7B}.
HELIX 132 148 {ECO:0000244|PDB:1H7B}.
TURN 149 155 {ECO:0000244|PDB:1H7B}.
HELIX 159 184 {ECO:0000244|PDB:1H7B}.
TURN 185 188 {ECO:0000244|PDB:1H79}.
STRAND 195 199 {ECO:0000244|PDB:1H7B}.
HELIX 205 220 {ECO:0000244|PDB:1H7B}.
TURN 223 226 {ECO:0000244|PDB:1H7B}.
STRAND 232 238 {ECO:0000244|PDB:1H7B}.
TURN 240 243 {ECO:0000244|PDB:1H7B}.
HELIX 251 264 {ECO:0000244|PDB:1H7B}.
STRAND 268 271 {ECO:0000244|PDB:1H7B}.
HELIX 272 279 {ECO:0000244|PDB:1H7B}.
TURN 289 291 {ECO:0000244|PDB:1H7B}.
STRAND 310 318 {ECO:0000244|PDB:1H7B}.
HELIX 319 324 {ECO:0000244|PDB:1H7B}.
HELIX 334 358 {ECO:0000244|PDB:1H7B}.
TURN 359 361 {ECO:0000244|PDB:1H7B}.
HELIX 364 366 {ECO:0000244|PDB:1H7B}.
HELIX 368 371 {ECO:0000244|PDB:1H7B}.
STRAND 384 386 {ECO:0000244|PDB:1H7B}.
HELIX 387 390 {ECO:0000244|PDB:1H7B}.
TURN 391 394 {ECO:0000244|PDB:1H7B}.
STRAND 395 402 {ECO:0000244|PDB:1H7B}.
HELIX 404 411 {ECO:0000244|PDB:1H7B}.
HELIX 416 434 {ECO:0000244|PDB:1H7B}.
STRAND 437 441 {ECO:0000244|PDB:1H7B}.
HELIX 448 460 {ECO:0000244|PDB:1H7B}.
TURN 464 467 {ECO:0000244|PDB:1H7B}.
STRAND 468 471 {ECO:0000244|PDB:1H7B}.
STRAND 480 482 {ECO:0000244|PDB:1H78}.
HELIX 486 493 {ECO:0000244|PDB:1H7B}.
HELIX 494 498 {ECO:0000244|PDB:1H7B}.
STRAND 506 509 {ECO:0000244|PDB:1H7B}.
HELIX 517 530 {ECO:0000244|PDB:1H7B}.
STRAND 532 537 {ECO:0000244|PDB:1H7B}.
STRAND 540 542 {ECO:0000244|PDB:1H7B}.
TURN 544 546 {ECO:0000244|PDB:1HK8}.
STRAND 553 555 {ECO:0000244|PDB:1H7A}.
STRAND 556 560 {ECO:0000244|PDB:1HK8}.
STRAND 562 564 {ECO:0000244|PDB:1HK8}.
HELIX 569 571 {ECO:0000244|PDB:1HK8}.
STRAND 573 576 {ECO:0000244|PDB:1H7B}.
STRAND 578 581 {ECO:0000244|PDB:1H7B}.
SEQUENCE 605 AA; 67957 MW; C5F29CE03126800B CRC64;
MTIEKEIEGL IHKTNKDLLN ENANKDSRVF PTQRDLMAGI VSKHIAKNMV PSFIMKAHES
GIIHVHDIDY SPALPFTNCC LVDLKGMLEN GFKLGNAQIE TPKSIGVATA IMAQITAQVA
SHQYGGTTFA NVDKVLSPYV KRTYAKHIED AEKWQIADAL NYAQSKTEKD VYDAFQAYEY
EVNTLFSSNG QTPFVTITFG TGTDWTERMI QKAILKNRIK GLGRDGITPI FPKLVMFVEE
GVNLYKDDPN YDIKQLALEC ASKRMYPDII SAKNNKAITG SSVPVSPMGC RSFLSVWKDS
TGNEILDGRN NLGVVTLNLP RIALDSYIGT QFNEQKFVEL FNERMDLCFE ALMCRISSLK
GVKATVAPIL YQEGAFGVRL KPDDDIIELF KNGRSSVSLG YIGIHELNIL VGRDIGREIL
TKMNAHLKQW TERTGFAFSL YSTPAENLCY RFCKLDTEKY GSVKDVTDKG WYTNSFHVSV
EENITPFEKI SREAPYHFIA TGGHISYVEL PDMKNNLKGL EAVWDYAAQH LDYFGVNMPV
DKCFTCGSTH EMTPTENGFV CSICGETDPK KMNTIRRTCG YLGNPNERGF NLGKNKEIMH
RVKHQ


Related products :

Catalog number Product name Quantity
CSB-RP159874Ba Recombinant Escherichia coli Anaerobic ribonucleoside-triphosphate reductase 500ug
CSB-RP159874Ba Recombinant Escherichia coli Anaerobic ribonucleoside-triphosphate reductase Source: E.coli 1mg
E0190h ELISA kit Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
U0190h CLIA Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
E0190h ELISA Homo sapiens,Human,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,RR1,RRM1 96T
E0190m ELISA Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
E0190m ELISA kit Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
U0190m CLIA Mouse,Mus musculus,Ribonucleoside-diphosphate reductase large subunit,Ribonucleoside-diphosphate reductase subunit M1,Ribonucleotide reductase large subunit,Rrm1 96T
EIAAB34887 Homo sapiens,Human,Ribonucleoside-diphosphate reductase subunit M2,Ribonucleotide reductase small chain,Ribonucleotide reductase small subunit,RR2,RRM2
18-661-15107 Ribonucleoside-diphosphate reductase M2 subunit B - EC 1.17.4.1; TP53-inducible ribonucleotide reductase M2 B; p53-inducible ribonucleotide reductase small subunit 2-like protein; p53R2 Polyclonal 0.1 mg
EIAAB34888 Mouse,Mus musculus,Ribonucleoside-diphosphate reductase subunit M2,Ribonucleotide reductase small chain,Ribonucleotide reductase small subunit,Rrm2
EIAAB34886 Rat,Rattus norvegicus,Ribonucleoside-diphosphate reductase subunit M2,Ribonucleotide reductase small chain,Ribonucleotide reductase small subunit,Rrm2
EIAAB34889 Homo sapiens,Human,p53-inducible ribonucleotide reductase small subunit 2-like protein,p53R2,P53R2,Ribonucleoside-diphosphate reductase subunit M2 B,RRM2B,TP53-inducible ribonucleotide reductase M2 B
EIAAB34890 Mouse,Mus musculus,p53-inducible ribonucleotide reductase small subunit 2-like protein,p53R2,P53r2,Ribonucleoside-diphosphate reductase subunit M2 B,Rrm2b,TP53-inducible ribonucleotide reductase M2 B
15-288-22152A Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain Polyclonal 0.05 mg
15-288-22152A Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain Polyclonal 0.1 mg
ER473 Ribonucleoside-diphosphate reductase subunit M2 Elisa Kit 96T
EH1395 Ribonucleoside-diphosphate reductase subunit M2 Elisa Kit 96T
10-288-22152F Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain 0.1 mg
10-288-22152F Ribonucleoside-diphosphate reductase M2 subunit - EC 1.17.4.1; Ribonucleotide reductase small subunit; Ribonucleotide reductase small chain 0.05 mg
G7932 Ribonucleoside-diphosphate reductase subunit M2 (RRM2), Rat, ELISA Kit 96T
CSB-EL020519RA Rat Ribonucleoside-diphosphate reductase subunit M2(RRM2) ELISA kit 96T
EH756 Ribonucleoside-diphosphate reductase large subunit Elisa Kit 96T
RIR2B_HUMAN Human ELISA Kit FOR Ribonucleoside-diphosphate reductase subunit M2 B 96T
E1201b Mouse ELISA Kit FOR Ribonucleoside-diphosphate reductase subunit M2 B 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur