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Q59490 (RTPR_LACLE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:rtpR
OrganismLactobacillus leichmannii
Taxonomic identifier28039 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Adenosylcobalamin.

Enzyme regulation

Allosterically regulated by ATP and dNTP.

Subunit structure

Monomer.

Sequence similarities

Belongs to the class II ribonucleoside-triphosphate reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 739738Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase
PRO_0000221428

Regions

Region147 – 15812Effector region-1
Region168 – 313146Effector region-2
Region565 – 62662Adenosylcobalamin-binding-1
Region685 – 72440Adenosylcobalamin-binding-2

Sites

Active site4081
Active site4101

Amino acid modifications

Disulfide bond119 ↔ 419Redox-active

Experimental info

Sequence conflict1521F → C in AAA03078. Ref.1
Sequence conflict7171N → D AA sequence Ref.1

Secondary structure

............................................................................................................................... 739
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59490 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8B04C6A5EADB6D6E

FASTA73981,983
        10         20         30         40         50         60 
MSEEISLSAE FIDRVKASVK PHWGKLGWVT YKRTYARWLP EKGRSENWDE TVKRVVEGNI 

        70         80         90        100        110        120 
NLDPRLQDSP SLELKQSLTE EAERLYKLIY GLGATPSGRN LWISGTDYQR RTGDSLNNCW 

       130        140        150        160        170        180 
FVAIRPQKYG DSKIVPSYLG KQEKAVSMPF SFLFDELMKG GGVGFSVARS NISQIPRVDF 

       190        200        210        220        230        240 
AIDLQLVVDE TSESYDASVK VGAVGKNELV QDADSIYYRL PDTREGWVLA NALLIDLHFA 

       250        260        270        280        290        300 
QTNPDRKQKL ILDLSDIRPY GAEIHGFGGT ASGPMPLISM LLDVNEVLNN KAGGRLTAVD 

       310        320        330        340        350        360 
AADICNLIGK AVVAGNVRRS AELALGSNDD QDFISMKQDQ EKLMHHRWAS NNSVAVDSAF 

       370        380        390        400        410        420 
SGYQPIAAGI RENGEPGIVN LDLSKNYGRI VDGYQAGIDG DVEGTNPCGE ISLANGEPCN 

       430        440        450        460        470        480 
LFEVFPLIAE EQGWDLQEVF ALAARYAKRV TFSPYDWEIS REIIQKNRRI GISMSGIQDW 

       490        500        510        520        530        540 
LLTRLGNRVV TGFKDDFDPE THEAIKVPVY DKRAIKMVDQ LYKAVVKADQ DYSKTLGCNE 

       550        560        570        580        590        600 
SIKHTTVKPS GTVAKLAGAS EGMHFHYGAY LIQRIRFQDS DPLLPALKAC GYRTEADIYT 

       610        620        630        640        650        660 
ENTTCVEFPI KAVGADNPNF ASAGTVSIAE QFATQAFLQT YWSDNAVSCT ITFQDSEGDQ 

       670        680        690        700        710        720 
VESLLRQYRF ITKSTSLLPY FGGSLQQAPK EPIDKETYEK RSQEITGNVE EVFSQLNSDV 

       730 
KDLELVDQTD CEGGACPIK 

« Hide

References

[1]"Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii."
Booker S., Stubbe J.
Proc. Natl. Acad. Sci. U.S.A. 90:8352-8356(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22; 112-121; 449-461; 489-513 AND 702-739.
[2]"Location of the redox-active thiols of ribonucleotide reductase: sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes."
Lin A.-N.I., Ashley G.W., Stubbe J.
Biochemistry 26:6905-6909(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 112-121 AND 722-739.
Strain: ATCC 7830.
[3]"The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer."
Sintchak M.D., Arjara G., Kellogg B.A., Stubbe J., Drennan C.L.
Nat. Struct. Biol. 9:293-300(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADENINYLPENTYLCOBALAMIN, SEQUENCE REVISION TO 151.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20047 Unassigned DNA. Translation: AAA03078.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1LX-ray1.75A/B/C/D1-739[»]
ProteinModelPortalQ59490.
SMRQ59490. Positions 4-724.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ59490.

Family and domain databases

InterProIPR000788. RNR_lg_C.
IPR013345. RTP_Rdtase_AdoCbl-dep.
[Graphical view]
PfamPF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view]
TIGRFAMsTIGR02505. RTPR. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ59490.

Entry information

Entry nameRTPR_LACLE
AccessionPrimary (citable) accession number: Q59490
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 72 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references