RIR1_BPT4
ID RIR1_BPT4 Reviewed; 754 AA.
AC P32282;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Protein B1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=NRDA;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2846540; DOI=10.1016/s0021-9258(18)37585-9;
RA Tseng M.J., Hilfinger J.M., Walsh A., Greenberg G.R.;
RT "Total sequence, flanking regions, and transcripts of bacteriophage T4 nrdA
RT gene, coding for alpha chain of ribonucleoside diphosphate reductase.";
RL J. Biol. Chem. 263:16242-16251(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.
RX PubMed=3322944; DOI=10.1016/0378-1119(87)90185-5;
RA Chu F.K., Maley G.F., Wang A.M., Maley F.;
RT "Localization of the T4 phage ribonucleotide reductase B1 subunit gene and
RT the nucleotide sequence of its upstream and 5' coding regions.";
RL Gene 57:143-148(1987).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC -!- ACTIVITY REGULATION: Under complex allosteric control mediated by
CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide
CC bound at the specificity site determines substrate preference. It seems
CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP
CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000305}.
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DR EMBL; J03968; AAA32527.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42621.1; -; Genomic_DNA.
DR EMBL; M22627; AAA32531.1; -; Genomic_DNA.
DR RefSeq; NP_049845.1; NC_000866.4.
DR SMR; P32282; -.
DR PRIDE; P32282; -.
DR GeneID; 1258795; -.
DR KEGG; vg:1258795; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 1.
DR Pfam; PF03477; ATP-cone; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 1.
DR PROSITE; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis;
KW Disulfide bond; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..754
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187226"
FT DOMAIN 4..93
FT /note="ATP-cone"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT REGION 621..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 437
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 221..222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 435..439
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 615..619
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 222
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 229
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 259
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 457
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 726
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 727
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 749
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 752
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 222..457
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ 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
