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Ribonucleoside-diphosphate reductase subunit alpha (EC 1.17.4.1) (Protein B1) (Ribonucleotide reductase)

 RIR1_BPT4               Reviewed;         754 AA.
P32282;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
27-SEP-2017, entry version 103.
RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
EC=1.17.4.1;
AltName: Full=Protein B1;
AltName: Full=Ribonucleotide reductase;
Name=NRDA;
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].
PubMed=2846540;
Tseng M.J., Hilfinger J.M., Walsh A., Greenberg G.R.;
"Total sequence, flanking regions, and transcripts of bacteriophage T4
nrdA gene, coding for alpha chain of ribonucleoside diphosphate
reductase.";
J. Biol. Chem. 263:16242-16251(1988).
[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 1-66.
PubMed=3322944; DOI=10.1016/0378-1119(87)90185-5;
Chu F.K., Maley G.F., Wang A.M., Maley F.;
"Localization of the T4 phage ribonucleotide reductase B1 subunit gene
and the nucleotide sequence of its upstream and 5' coding regions.";
Gene 57:143-148(1987).
-!- FUNCTION: Provides the precursors necessary for DNA synthesis.
Catalyzes the biosynthesis of deoxyribonucleotides from the
corresponding ribonucleotides.
-!- CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate +
thioredoxin disulfide + H(2)O = ribonucleoside diphosphate +
thioredoxin.
-!- ENZYME REGULATION: Under complex allosteric control mediated by
deoxynucleoside triphosphates and ATP binding. 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
(By similarity). {ECO:0000250}.
-!- PATHWAY: Genetic information processing; DNA replication.
-!- SUBUNIT: Heterodimer of a large and a small subunit.
-!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase
large chain family. {ECO:0000305}.
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EMBL; J03968; AAA32527.1; -; Genomic_DNA.
EMBL; AF158101; AAD42621.1; -; Genomic_DNA.
EMBL; M22627; AAA32531.1; -; Genomic_DNA.
RefSeq; NP_049845.1; NC_000866.4.
ProteinModelPortal; P32282; -.
SMR; P32282; -.
PRIDE; P32282; -.
GeneID; 1258795; -.
KEGG; vg:1258795; -.
OrthoDB; VOG0900001D; -.
UniPathway; UPA00326; -.
Proteomes; UP000009087; Genome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:CACAO.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
InterPro; IPR005144; ATP-cone_dom.
InterPro; IPR013346; NrdE_NrdA.
InterPro; IPR000788; RNR_lg_C.
InterPro; IPR013509; RNR_lsu_N.
InterPro; IPR008926; RNR_R1-su_N.
Pfam; PF03477; ATP-cone; 1.
Pfam; PF02867; Ribonuc_red_lgC; 1.
Pfam; PF00317; Ribonuc_red_lgN; 1.
PRINTS; PR01183; RIBORDTASEM1.
SUPFAM; SSF48168; SSF48168; 1.
TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
PROSITE; PS51161; ATP_CONE; 1.
PROSITE; PS00089; RIBORED_LARGE; 1.
3: Inferred from homology;
Allosteric enzyme; ATP-binding; Complete proteome; Disulfide bond;
DNA replication; Nucleotide-binding; Oxidoreductase;
Reference proteome.
CHAIN 1 754 Ribonucleoside-diphosphate reductase
subunit alpha.
/FTId=PRO_0000187226.
DOMAIN 4 93 ATP-cone. {ECO:0000255|PROSITE-
ProRule:PRU00492}.
REGION 221 222 Substrate binding. {ECO:0000250}.
REGION 435 439 Substrate binding. {ECO:0000250}.
REGION 615 619 Substrate binding. {ECO:0000250}.
ACT_SITE 435 435 Proton acceptor. {ECO:0000250}.
ACT_SITE 437 437 Cysteine radical intermediate.
{ECO:0000250}.
ACT_SITE 439 439 Proton acceptor. {ECO:0000250}.
BINDING 206 206 Substrate. {ECO:0000250}.
BINDING 250 250 Substrate; via amide nitrogen.
{ECO:0000250}.
SITE 222 222 Important for hydrogen atom transfer.
{ECO:0000250}.
SITE 229 229 Allosteric effector binding.
{ECO:0000250}.
SITE 259 259 Allosteric effector binding.
{ECO:0000250}.
SITE 457 457 Important for hydrogen atom transfer.
{ECO:0000250}.
SITE 726 726 Important for electron transfer.
{ECO:0000250}.
SITE 727 727 Important for electron transfer.
{ECO:0000250}.
SITE 749 749 Interacts with thioredoxin/glutaredoxin.
{ECO:0000250}.
SITE 752 752 Interacts with thioredoxin/glutaredoxin.
{ECO:0000250}.
DISULFID 222 457 Redox-active. {ECO:0000250}.
SEQUENCE 754 AA; 85973 MW; 31D178EAA580068A CRC64;
MQLINVIKSS GVSQSFDPQK IIKVLSWAAE GTSVDPYELY ENIKSYLRDG MTTDDIQTIV
IKAAANSISV EEPDYQYVAA RCLMFALRKH VYGQYEPRSF IDHISYCVNA GKYDPELLSK
YSAEEITFLE SKIKHERDME FTYSGAMQLK EKYLVKDKTT GQIYETPQFA FMTIGMALHQ
DEPVDRLKHV IRFYEAVSTR QISLPTPIMA GCRTPTRQFS SCVVIEAGDS LKSINKASAS
IVEYISKRAG IGINVGMIRA EGSKIGMGEV RHTGVIPFWK HFQTAVKSCS QGGIRGGAAT
AYYPIWHLEV ENLLVLKNNK GVEENRIRHM DYGVQLNDLM MERFGKNDYI TLFSPHEMGG
ELYYSYFKDQ DRFRELYEAA EKDPNIRKKR IKARELFELL MTERSGTARI YVQFIDNTNN
YTPFIREKAP IRQSNLCCEI AIPTNDVNSP DAEIGLCTLS AFVLDNFDWQ DQDKINELAE
VQVRALDNLL DYQGYPVPEA EKAKKRRNLG VGVTNYAAWL ASNFASYEDA NDLTHELFER
LQYGLIKASI KLAKEKGPSE YYSDTRWSRG ELPIDWYNKK IDQIAAPKYV CDWSALREDL
KLFGIRNSTL SALMPCESSS QVSNSTNGYE PPRGPVSVKE SKEGSFNQVV PNIEHNIDLY
DYTWKLAKKG NKPYLTQVAI MLKWVCQSAS ANTYYDPQIF PKGKVPMSIM IDDMLYGWYY
GIKNFYYHNT RDGSGTDDYE IETPKADDCA ACKL


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