P32282 (RIR1_BPT4) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase subunit alpha
EC=1.17.4.1

Alternative name(s):
Protein B1
Ribonucleotide reductase

Gene names

Name:

NRDA

Organism

Enterobacteria phage T4 (Bacteriophage T4) [Reference proteome]

Taxonomic identifier

10665 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › Tevenvirinae › T4likevirus › Enterobacteria phage T4 sensu lato

Virus host

Escherichia coli [TaxID: 562]

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = 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.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small subunit.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain.

Ontologies

Keywords
Biological process	DNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 754	754	Ribonucleoside-diphosphate reductase subunit alpha		PRO_0000187226
Regions
	Domain	4 – 93	90	ATP-cone
	Region	221 – 222	2	Substrate binding By similarity
	Region	435 – 439	5	Substrate binding By similarity
	Region	615 – 619	5	Substrate binding By similarity
Sites
	Active site	435	1	Proton acceptor By similarity
	Active site	437	1	Cysteine radical intermediate By similarity
	Active site	439	1	Proton acceptor By similarity
	Binding site	206	1	Substrate By similarity
	Binding site	250	1	Substrate; via amide nitrogen By similarity
	Site	222	1	Important for hydrogen atom transfer By similarity
	Site	229	1	Allosteric effector binding By similarity
	Site	259	1	Allosteric effector binding By similarity
	Site	457	1	Important for hydrogen atom transfer By similarity
	Site	726	1	Important for electron transfer By similarity
	Site	727	1	Important for electron transfer By similarity
	Site	749	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	752	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	222 ↔ 457		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P32282 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 31D178EAA580068A	FASTA	754	85,973
	10 20 30 40 50 60 MQLINVIKSS GVSQSFDPQK IIKVLSWAAE GTSVDPYELY ENIKSYLRDG MTTDDIQTIV 70 80 90 100 110 120 IKAAANSISV EEPDYQYVAA RCLMFALRKH VYGQYEPRSF IDHISYCVNA GKYDPELLSK 130 140 150 160 170 180 YSAEEITFLE SKIKHERDME FTYSGAMQLK EKYLVKDKTT GQIYETPQFA FMTIGMALHQ 190 200 210 220 230 240 DEPVDRLKHV IRFYEAVSTR QISLPTPIMA GCRTPTRQFS SCVVIEAGDS LKSINKASAS 250 260 270 280 290 300 IVEYISKRAG IGINVGMIRA EGSKIGMGEV RHTGVIPFWK HFQTAVKSCS QGGIRGGAAT 310 320 330 340 350 360 AYYPIWHLEV ENLLVLKNNK GVEENRIRHM DYGVQLNDLM MERFGKNDYI TLFSPHEMGG 370 380 390 400 410 420 ELYYSYFKDQ DRFRELYEAA EKDPNIRKKR IKARELFELL MTERSGTARI YVQFIDNTNN 430 440 450 460 470 480 YTPFIREKAP IRQSNLCCEI AIPTNDVNSP DAEIGLCTLS AFVLDNFDWQ DQDKINELAE 490 500 510 520 530 540 VQVRALDNLL DYQGYPVPEA EKAKKRRNLG VGVTNYAAWL ASNFASYEDA NDLTHELFER 550 560 570 580 590 600 LQYGLIKASI KLAKEKGPSE YYSDTRWSRG ELPIDWYNKK IDQIAAPKYV CDWSALREDL 610 620 630 640 650 660 KLFGIRNSTL SALMPCESSS QVSNSTNGYE PPRGPVSVKE SKEGSFNQVV PNIEHNIDLY 670 680 690 700 710 720 DYTWKLAKKG NKPYLTQVAI MLKWVCQSAS ANTYYDPQIF PKGKVPMSIM IDDMLYGWYY 730 740 750 GIKNFYYHNT RDGSGTDDYE IETPKADDCA ACKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Total sequence, flanking regions, and transcripts of bacteriophage T4 nrdA gene, coding for alpha chain of ribonucleoside diphosphate reductase." Tseng M.J., Hilfinger J.M., Walsh A., Greenberg G.R. J. Biol. Chem. 263:16242-16251(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Bacteriophage T4 genome." Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W. Microbiol. Mol. Biol. Rev. 67:86-156(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Localization of the T4 phage ribonucleotide reductase B1 subunit gene and the nucleotide sequence of its upstream and 5' coding regions." Chu F.K., Maley G.F., Wang A.M., Maley F. Gene 57:143-148(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-66.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03968 Genomic DNA. Translation: AAA32527.1. AF158101 Genomic DNA. Translation: AAD42621.1. M22627 Genomic DNA. Translation: AAA32531.1.
RefSeq	NP_049845.1. NC_000866.4.
3D structure databases
ProteinModelPortal	P32282.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1258795.
Phylogenomic databases
ProtClustDB	PHA2572.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR008926. RNR_R1-su_N. [Graphical view]
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
SUPFAM	SSF48168. Ribonucleo_red_N. 1 hit.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS51161. ATP_CONE. 1 hit. PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_BPT4

Accession

Primary (citable) accession number: P32282

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program