Reviewed, UniProtKB/Swiss-Prot Q9SJ20 (RIR1_ARATH)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase large subunit
    EC=1.17.4.1
Alternative name(s):
    Ribonucleoside-diphosphate reductase R1 subunit
      Short name=AtRNR1

Gene names

Name:	RNR1
Ordered Locus Names:	At2g21790
ORF Names:	F7D8.11

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	816 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.1
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.
Enzyme regulation	Allosterically regulated by nucleoside triphosphates, stimulated by ATP and inhibited by dATP. ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Ref.1
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterotetramer of two large/R1 and two small/R2 subunits. A radical transfer pathway may occur between 'Tyr-125' of protein R2 and R1. Ref.1
Subcellular location	Cytoplasm By similarity.
Induction	Basal expression regulated by ATR/RAD3. Can be induced by another pathway when dNTPs levels are low. Ref.4
Post-translational modification	Contains a disulfide bonds Probable. Binding of the substrate occurs primarily when the active-site cysteines are reduced.
Miscellaneous	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.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family. Contains 1 ATP-cone domain.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from mutant phenotype. Source: TAIR deoxyribonucleoside triphosphate biosynthetic process Inferred from mutant phenotype. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR
Cellular component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro ribonucleoside-diphosphate reductase activity 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 – 816	816	Ribonucleoside-diphosphate reductase large subunit		PRO_0000187195
Regions
	Domain	1 – 92	92	ATP-cone
Sites
	Active site	218	1	Hydrogen atom transfer By similarity
	Active site	427	1	Proton acceptor By similarity
	Active site	429	1	Proton acceptor By similarity
	Active site	431	1	Proton acceptor By similarity
	Active site	444	1	Hydrogen atom transfer By similarity
	Active site	756	1	Electron transfer By similarity
	Active site	757	1	Electron transfer By similarity
	Site	226	1	Allosteric effector binding By similarity
	Site	256	1	Allosteric effector binding By similarity
	Site	811	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	814	1	Interacts with thioredoxin/glutaredoxin By similarity
Experimental info
	Sequence conflict	37	1	V → I in AAC61773. Ref.1
	Sequence conflict	233	1	E → G in AAC61773. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9SJ20-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: A6769E2F210488EA	FASTA	816	91,816
	10 20 30 40 50 60 MYVVKRDGRQ ETVHFDKITA RLKKLSYGLS SDHCDPVLVA QKVCAGVYKG VTTSQLDELA 70 80 90 100 110 120 AETAAAMTCN HPDYASLAAR IAVSNLHKNT KKSFSETIKD MFYHVNDRSG LKSPLIADDV 130 140 150 160 170 180 FEIIMQNAAR LDSEIIYDRD FEYDYFGFKT LERSYLLKVQ GTVVERPQHM LMRVAVGIHK 190 200 210 220 230 240 DDIDSVIQTY HLMSQRWFTH ASPTLFNAGT PRPQLSSCFL VCMKDDSIEG IYETLKECAV 250 260 270 280 290 300 ISKSAGGIGV SVHNIRATGS YIRGTNGTSN GIVPMLRVFN DTARYVDQGG GKRKGAFAVY 310 320 330 340 350 360 LEPWHADVYE FLELRKNHGK EEHRARDLFY ALWLPDLFME RVQNNGQWSL FCPNEAPGLA 370 380 390 400 410 420 DCWGAEFETL YTKYEREGKA KKVVQAQQLW YEILTSQVET GTPYMLFKDS CNRKSNQQNL 430 440 450 460 470 480 GTIKSSNLCT EIIEYTSPTE TAVCNLASIA LPRFVREKGV PLDSHPPKLA GSLDSKNRYF 490 500 510 520 530 540 DFEKLAEVTA TVTVNLNKII DVNYYPVETA KTSNMRHRPI GIGVQGLADA FILLGMPFDS 550 560 570 580 590 600 PEAQQLNKDI FETIYYHALK ASTELAARLG PYETYAGSPV SKGILQPDMW NVIPSDRWDW 610 620 630 640 650 660 AVLRDMISKN GVRNSLLVAP MPTASTSQIL GNNECFEPYT SNIYSRRVLS GEFVVVNKHL 670 680 690 700 710 720 LHDLTDMGLW TPTLKNKLIN ENGSIVNVAE IPDDLKAIYR TVWEIKQRTV VDMAADRGCY 730 740 750 760 770 780 IDQSQSLNIH MDKPNFAKLT SLHFYTWKKG LKTGMYYLRS RAAADAIKFT VDTAMLKEKP 790 800 810 SVAEGDKEVE EEDNETKLAQ MVCSLTNPEE CLACGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An active ribonucleotide reductase from Arabidopsis thaliana cloning, expression and characterization of the large subunit." Sauge-Merle S., Falconet D., Fontecave M. Eur. J. Biochem. 266:62-69(1999) [PubMed: 10542051] [Abstract] Cited for: NUCLEOTIDE SEQUENCE, FUNCTION, SUBUNIT, ENZYME REGULATION. Tissue: Callus.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"ATR regulates a G2-phase cell-cycle checkpoint in Arabidopsis thaliana." Culligan K., Tissier A., Britt A. Plant Cell 16:1091-1104(2004) [PubMed: 15075397] [Abstract] Cited for: INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF092841 mRNA. Translation: AAC61773.1. AC007019 Genomic DNA. Translation: AAD20398.1. AY035080 mRNA. Translation: AAK59585.1. BT008573 mRNA. Translation: AAP40400.1.
IPI	IPI00525243.
PIR	B84605. T51813.
RefSeq	NP_179770.1.
UniGene	At.115
3D structure databases
HSSP	HSSP built from PDB template 5R1R based on UniProtKB P00452.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9SJ20.
Proteomic databases
PRIDE	Q9SJ20.
Genome annotation databases
GeneID	816715.
GenomeReviews	Gene locus AT2G21790 in contig CT485783_GR.
KEGG	ath:AT2G21790.
NMPDR	fig|3702.1.peg.28942.
Organism-specific databases
GeneFarm	2079.
TAIR	At2g21790.
Phylogenomic databases
OMA	GSLWSKG.
Enzyme and pathway databases
BRENDA	1.17.4.1. 302.
Gene expression databases
ArrayExpress	Q9SJ20.
Genevestigator	Q9SJ20.
GermOnline	AT2G21790. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. [Graphical view]
PANTHER	PTHR11573. Ribncl_red_lg_C. 1 hit.
Pfam	PF03477. ATP-cone. 1 hit. PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
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_ARATH

Accession

Primary (citable) accession number: Q9SJ20
Secondary accession number(s): O82573

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)