Q8SR37 (RIR1_ENCCU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase large chain
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase

Gene names

Ordered Locus Names:

ECU10_0920

Organism

Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) [Reference proteome]

Taxonomic identifier

284813 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Microsporidia › Apansporoblastina › Unikaryonidae › Encephalitozoon › Encephalitozoon cuniculi

Protein attributes

Sequence length	768 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 to separate specificity and activation sites on the large subunit. 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. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Heterodimer of a large and a small subunit By similarity.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family.

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 deoxyribonucleotide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 768	768	Ribonucleoside-diphosphate reductase large chain		PRO_0000187200
Regions
	Region	211 – 212	2	Substrate binding By similarity
	Region	279 – 282	4	Allosteric effector binding, determines substrate specificity By similarity
	Region	420 – 424	5	Substrate binding By similarity
	Region	595 – 599	5	Substrate binding By similarity
Sites
	Active site	420	1	Proton acceptor By similarity
	Active site	422	1	Cysteine radical intermediate By similarity
	Active site	424	1	Proton acceptor By similarity
	Binding site	196	1	Substrate By similarity
	Binding site	241	1	Substrate; via amide nitrogen By similarity
	Site	212	1	Important for hydrogen atom transfer By similarity
	Site	220	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	250	1	Allosteric effector binding, determines substrate specificity By similarity
	Site	437	1	Important for hydrogen atom transfer By similarity
	Site	729	1	Important for electron transfer By similarity
	Site	730	1	Important for electron transfer By similarity
	Site	763	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	766	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	212 ↔ 437		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8SR37 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 3E6BF6826805E20D	FASTA	768	87,941
	10 20 30 40 50 60 MENFSNSKRI KSEKLGIDLI RSRIEGYVKD LKLRHVDVDE LVERIVSGWC EDMTRKETID 70 80 90 100 110 120 YCSETAASMI TKHPEYGQIS SRIIVSYIHE ITMDSFVEKI KYIQKHRGMV SEEMYGIILE 130 140 150 160 170 180 HGETIEGMIN YENDFLFSYF GILTLMKSYL IKVGEEIIER PQDMFMRVAL QIHKTDFEKV 190 200 210 220 230 240 REVYNLLSGH YFTHATPTLY NSCLKNPQLA SCFLITPRED SIEGVYHMIN QAAIITKYSG 250 260 270 280 290 300 GIGLNLHGIR SKGSSLRSTG GRSNGIIPLI QVLNATKRYI NQGAERRPGS IAIFLEPWHM 310 320 330 340 350 360 EIFDFLELRK NTGPEEFRAR DIFTALWIND LFMERVKNNE EWSLFCPSQA VGLSDVWGEE 370 380 390 400 410 420 FNALYCKYEK TISRTVVPAQ KLWKAIIEAQ IETGTPYMCY KDACNRLSNQ QHLGTIKSSN 430 440 450 460 470 480 LCAEIVEYSS GEETSVCNLA SICLPMFVKD GWFDFEAFRR VVKILTVNLN RVIDFNYYPV 490 500 510 520 530 540 EEARRSNMRN RPIGIGVQGL ADLFAILRLA FESDGARSLN QDIFEAMYYS AMEASCELAE 550 560 570 580 590 600 KEGPFPSYEG SPISKGIFHF ELAGRKASGN WDWEGLRERI RRHGVRNSLL IALMPTAGTS 610 620 630 640 650 660 QIFGNNEAFE PHASNIYTRR THAGEFQIVN QHLVNDLVRL GLWSYEMKNL VIENEGSIQN 670 680 690 700 710 720 ITSIPHEIRE IYKTAWEIKM KSVIDLAADR QVFVDQSQSL NIFIAKPTYS QLTSMHFYGY 730 740 750 760 HCGLKTGMYY LRTRPITSAI KFTVDKKLAE KTLSSMNDTD DPCSMCSS

References

[1]

"Genome sequence and gene compaction of the eukaryote parasite Encephalitozoon cuniculi." Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F., Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P., Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J., Vivares C.P. Nature 414:450-453(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GB-M1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590449 Genomic DNA. Translation: CAD25811.1.
RefSeq	NP_586207.1. NM_001042040.1.
3D structure databases
ProteinModelPortal	Q8SR37.
SMR	Q8SR37. Positions 79-734.
ModBase	Search...
Protein-protein interaction databases
STRING	6035.ECU10_0920.
Proteomic databases
PRIDE	Q8SR37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	859856.
KEGG	ecu:ECU10_0920.
Phylogenomic databases
eggNOG	COG0209.
HOGENOM	HOG000057035.
KO	K10807.
OMA	YKYGVKT.
Enzyme and pathway databases
UniPathway	UPA00326.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR000788. RNR_lg_C. IPR013509. RNR_lsu_N. IPR008926. RNR_R1-su_N. [Graphical view]
Pfam	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	PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR1_ENCCU

Accession

Primary (citable) accession number: Q8SR37

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program