Reviewed, UniProtKB/Swiss-Prot P74240 (RIR1_SYNY3)

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase subunit alpha
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase

Gene names

Name:	nrdA
Ordered Locus Names:	slr1164

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	767 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 By similarity.
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	Tetramer of two alpha and two beta subunits By similarity.
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
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 – 767	767	Ribonucleoside-diphosphate reductase subunit alpha		PRO_0000187222
Regions
	Domain	31 – 120	90	ATP-cone
	Region	243 – 244	2	Substrate binding By similarity
	Region	460 – 464	5	Substrate binding By similarity
	Region	631 – 635	5	Substrate binding By similarity
Sites
	Active site	460	1	Proton acceptor By similarity
	Active site	462	1	Cysteine radical intermediate By similarity
	Active site	464	1	Proton acceptor By similarity
	Binding site	228	1	Substrate By similarity
	Binding site	272	1	Substrate; via amide nitrogen By similarity
	Site	244	1	Important for hydrogen atom transfer By similarity
	Site	251	1	Allosteric effector binding By similarity
	Site	281	1	Allosteric effector binding By similarity
	Site	478	1	Important for hydrogen atom transfer By similarity
	Site	745	1	Important for electron transfer By similarity
	Site	746	1	Important for electron transfer By similarity
	Site	762	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	765	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	244 ↔ 478		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P74240-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 147151C406A082C5	FASTA	767	85,637
	10 20 30 40 50 60 MHPTLISAPI SSSANDAHAG TSQGSHQGHR IQVIRRDGSS TPLNIGKIRA VVDWACLGLE 70 80 90 100 110 120 VNSIALEAGL TTRLREGIST REIQDNLISC ALEMCSPNEP DWRYVAGRLH VWSLWKDTLV 130 140 150 160 170 180 RRGYQYGQYL RTVQTKVTNG EYDSRILTYS EGELQEAGCW INSDWDTDYD YAGAVLLTSR 190 200 210 220 230 240 YLLPNELPQE ALLTCALLLA SVEAPDRRLQ WARRFYESIA ARRISLATPI LANLRVPGGS 250 260 270 280 290 300 LTSCFIVAME DNLESIFGEI TNAARISKNG GGVGVNVSRI RATGSWVMGK PNASGGVIPW 310 320 330 340 350 360 TKLLNDTAIA VNQGGRRAGA VTVGLDVWHL DVPEFLEMQA ENGDQRRKAY DIFPQLILPD 370 380 390 400 410 420 EFMRRVINKE DWTLVDPYEV REKMGIELAE LWGEQFEGAY REIESNLDTT ITLYKRINAR 430 440 450 460 470 480 ELFKQIMRTQ VETGMPYLSF KDTINKANPN KHLGYIPGTN LCCESFSNVT PGQDAHCCNL 490 500 510 520 530 540 VSLNLANLDL QDIAGVSQIA VRMLDNTIEL TAPPFADAKS HNNKYRTIGV GAMGLADWLA 550 560 570 580 590 600 KRRLNYDELA DINRLFEEIG YWCTQSSMEL AKERGAYPAF PGSDWQKGLL IGSKPVSWFQ 610 620 630 640 650 660 ANAAKPERWE KLSNDIQTHG IRNSHITAIA PNTSSSLVQG CTASILPVYS RFFYDKWAKG 670 680 690 700 710 720 TVPIAPPFIG NCFWFYPENK TMDQRKVVKA VAAIQQWTDT GISMELLFNL NAGIYFPEEP 730 740 750 760 ERSLNAKDIF DTLVMAWEAG CKAIYYIRTV QKDDFKDSSD GCVACAN

References

[1]

"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000022 Genomic DNA. Translation: BAA18334.1.
PIR	S75875.
RefSeq	NP_441654.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P74240. 3 interactions.
STRING	P74240.
Genome annotation databases
GeneID	954980.
GenomeReviews	Gene locus slr1164 in contig BA000022_GR.
KEGG	syn:slr1164.
NMPDR	fig|1148.1.peg.1755.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0209.
HOGENOM	HBG296647.
OMA	EYVSCYL.
PhylomeDB	P74240.
Enzyme and pathway databases
BioCyc	SSP1148:SLR1164-MONOMER.
Family and domain databases
InterPro	IPR005144. ATP-cone. IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR008926. Ribnucl_Rdtase_R1-su_N. [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_SYNY3

Accession

Primary (citable) accession number: P74240

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 1, 1997
Last modified:	February 9, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)