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Q2PDF6 (RTPR_EUGGR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase

Short name=RTPR
EC=1.17.4.2
Gene names
Name:rnr
OrganismEuglena gracilis
Taxonomic identifier3039 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaEuglenidaEuglenalesEuglenaceaeEuglena

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O = ribonucleoside triphosphate + thioredoxin. Ref.1

Cofactor

Adenosylcobalamin. Ref.1

Subunit structure

Monomer. Ref.1

Sequence similarities

Belongs to the class II ribonucleoside-triphosphate reductase family.

Ontologies

Keywords
   Biological processDNA replication
   DomainRedox-active center
   LigandCobalamin
Cobalt
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-triphosphate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase
PRO_0000326545

Sites

Active site4271 By similarity
Active site4291 By similarity

Amino acid modifications

Disulfide bond189 ↔ 438Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2PDF6 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 91F4F84D8B2E297C

FASTA72982,175
        10         20         30         40         50         60 
MAEKENVHPQ VISSFPTPSK ALKLSEKSSL KDVQTDNAAV PLVVDETSYP EPTCEFYGGL 

        70         80         90        100        110        120 
LGPQLPEAER FVLDPALVEE YRHKKPPFGF NGLGEVVYLR TYAREKDNGQ SEVWLDTVQR 

       130        140        150        160        170        180 
VVTGTFEVLQ HHVVNKLHCH WDAQKAKERS EDMFRRIFEM KFLPPGRGLW AMGSPICRKK 

       190        200        210        220        230        240 
GFAAALNNCA FVSTATLEKD RVGPFLFLMD ASMLGVGVGF DNAGAGSFTV PGPDDTQPTY 

       250        260        270        280        290        300 
KFMIPDKREG WVESLKRLLK AHFCHTADVE FDYSKIREMG TKLKTFGGTS SGPGPLINLH 

       310        320        330        340        350        360 
KSIRKILVGE KGKPISVTCI TDIMNLIGVC TVAGNIRRSA EIAFGEADCK EFLDLKSYET 

       370        380        390        400        410        420 
NPHRVEYGWA SNNSIFAKVG MDYSDACERV RTNGEPGFAW LSNMQAFSRM NGKPDYRDQR 

       430        440        450        460        470        480 
VLGGNPCLEQ SLESMELCCL VETFPDKHET LEDFKRTLYS ALLYAKTVTL LPLHWRESNE 

       490        500        510        520        530        540 
IMLRNRRIGC SVSGIAQFIT NRGLHELKTW LEEGYDILHQ YDCQISEWLC IRQSIKLTSV 

       550        560        570        580        590        600 
KPSGTISLVA GATPGVHYPE SCYYTRRLRM ARDSPLLERL IKAGYHVEPC CVAPDVTAIV 

       610        620        630        640        650        660 
EFPVAAGNSI RTTRDITMWE QLSLAAFMQR YWADNQVSAT ITFDPETEGL HLNQALQYFQ 

       670        680        690        700        710        720 
YQLKGISFLP RYPMGAFKQM PYEAITKEQY EEAIRKVKED VSLSSANAIA ETVEENQQTF 


CDNDRCIKL 

« Hide

References

[1]"Euglena gracilis ribonucleotide reductase: the eukaryote class II enzyme and the possible antiquity of eukaryote B12 dependence."
Torrents E., Trevisiol C., Rotte C., Hellman U., Martin W., Reichard P.
J. Biol. Chem. 281:5604-5611(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
Strain: SAG 1224-5/25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ620503 mRNA. Translation: CAF05662.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ2PDF6.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameRTPR_EUGGR
AccessionPrimary (citable) accession number: Q2PDF6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: February 7, 2006
Last modified: October 16, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families