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Q59490

- RTPR_LACLE

UniProt

Q59490 - RTPR_LACLE

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Protein

Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase

Gene

rtpR

Organism
Lactobacillus leichmannii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Enzyme regulationi

Allosterically regulated by ATP and dNTP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei408 – 4081
Active sitei410 – 4101

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. nucleotide binding Source: InterPro
  3. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: InterPro
  4. ribonucleoside-triphosphate reductase activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

SABIO-RKQ59490.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase (EC:1.17.4.2)
Short name:
RTPR
Gene namesi
Name:rtpR
OrganismiLactobacillus leichmannii
Taxonomic identifieri28039 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 739738Adenosylcobalamin-dependent ribonucleoside-triphosphate reductasePRO_0000221428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi119 ↔ 419Redox-active

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
739
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Helixi27 – 326Combined sources
Turni33 – 353Combined sources
Turni40 – 434Combined sources
Helixi48 – 6013Combined sources
Helixi64 – 674Combined sources
Helixi72 – 9019Combined sources
Beta strandi93 – 964Combined sources
Helixi98 – 1036Combined sources
Helixi107 – 1104Combined sources
Turni113 – 1164Combined sources
Beta strandi119 – 1235Combined sources
Helixi148 – 15811Combined sources
Beta strandi162 – 1665Combined sources
Helixi169 – 1724Combined sources
Beta strandi183 – 1875Combined sources
Helixi195 – 2006Combined sources
Turni206 – 2083Combined sources
Beta strandi216 – 2194Combined sources
Helixi224 – 23613Combined sources
Helixi240 – 2423Combined sources
Beta strandi249 – 2535Combined sources
Beta strandi267 – 2704Combined sources
Helixi275 – 28915Combined sources
Turni290 – 2934Combined sources
Helixi298 – 31316Combined sources
Beta strandi322 – 3276Combined sources
Helixi331 – 3355Combined sources
Helixi336 – 3383Combined sources
Helixi340 – 3456Combined sources
Helixi347 – 3493Combined sources
Beta strandi350 – 3567Combined sources
Helixi363 – 37311Combined sources
Beta strandi377 – 3804Combined sources
Helixi381 – 3866Combined sources
Helixi390 – 3923Combined sources
Turni396 – 4016Combined sources
Beta strandi402 – 4054Combined sources
Beta strandi411 – 4144Combined sources
Beta strandi421 – 4244Combined sources
Helixi426 – 4316Combined sources
Helixi436 – 45015Combined sources
Helixi458 – 46710Combined sources
Beta strandi471 – 4744Combined sources
Helixi477 – 4859Combined sources
Beta strandi489 – 4979Combined sources
Turni499 – 5013Combined sources
Beta strandi504 – 5107Combined sources
Helixi512 – 53625Combined sources
Beta strandi545 – 5473Combined sources
Helixi551 – 5577Combined sources
Beta strandi569 – 57810Combined sources
Helixi583 – 5897Combined sources
Beta strandi593 – 5964Combined sources
Beta strandi598 – 6003Combined sources
Beta strandi603 – 6119Combined sources
Turni613 – 6164Combined sources
Turni623 – 6253Combined sources
Helixi628 – 64114Combined sources
Beta strandi650 – 6534Combined sources
Helixi655 – 6606Combined sources
Helixi661 – 6677Combined sources
Turni668 – 6714Combined sources
Beta strandi673 – 6797Combined sources
Beta strandi689 – 6924Combined sources
Helixi695 – 70410Combined sources
Helixi709 – 71911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L1LX-ray1.75A/B/C/D1-739[»]
ProteinModelPortaliQ59490.
SMRiQ59490. Positions 4-724.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59490.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 15812Effector region-1Add
BLAST
Regioni168 – 313146Effector region-2Add
BLAST
Regioni565 – 62662Adenosylcobalamin-binding-1Add
BLAST
Regioni685 – 72440Adenosylcobalamin-binding-2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Family and domain databases

InterProiIPR000788. RNR_lg_C.
IPR013345. RTP_Rdtase_AdoCbl-dep.
[Graphical view]
PfamiPF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02505. RTPR. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q59490-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEEISLSAE FIDRVKASVK PHWGKLGWVT YKRTYARWLP EKGRSENWDE
60 70 80 90 100
TVKRVVEGNI NLDPRLQDSP SLELKQSLTE EAERLYKLIY GLGATPSGRN
110 120 130 140 150
LWISGTDYQR RTGDSLNNCW FVAIRPQKYG DSKIVPSYLG KQEKAVSMPF
160 170 180 190 200
SFLFDELMKG GGVGFSVARS NISQIPRVDF AIDLQLVVDE TSESYDASVK
210 220 230 240 250
VGAVGKNELV QDADSIYYRL PDTREGWVLA NALLIDLHFA QTNPDRKQKL
260 270 280 290 300
ILDLSDIRPY GAEIHGFGGT ASGPMPLISM LLDVNEVLNN KAGGRLTAVD
310 320 330 340 350
AADICNLIGK AVVAGNVRRS AELALGSNDD QDFISMKQDQ EKLMHHRWAS
360 370 380 390 400
NNSVAVDSAF SGYQPIAAGI RENGEPGIVN LDLSKNYGRI VDGYQAGIDG
410 420 430 440 450
DVEGTNPCGE ISLANGEPCN LFEVFPLIAE EQGWDLQEVF ALAARYAKRV
460 470 480 490 500
TFSPYDWEIS REIIQKNRRI GISMSGIQDW LLTRLGNRVV TGFKDDFDPE
510 520 530 540 550
THEAIKVPVY DKRAIKMVDQ LYKAVVKADQ DYSKTLGCNE SIKHTTVKPS
560 570 580 590 600
GTVAKLAGAS EGMHFHYGAY LIQRIRFQDS DPLLPALKAC GYRTEADIYT
610 620 630 640 650
ENTTCVEFPI KAVGADNPNF ASAGTVSIAE QFATQAFLQT YWSDNAVSCT
660 670 680 690 700
ITFQDSEGDQ VESLLRQYRF ITKSTSLLPY FGGSLQQAPK EPIDKETYEK
710 720 730
RSQEITGNVE EVFSQLNSDV KDLELVDQTD CEGGACPIK
Length:739
Mass (Da):81,983
Last modified:January 23, 2007 - v4
Checksum:i8B04C6A5EADB6D6E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521F → C in AAA03078. (PubMed:8397403)Curated
Sequence conflicti717 – 7171N → D AA sequence (PubMed:8397403)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20047 Unassigned DNA. Translation: AAA03078.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20047 Unassigned DNA. Translation: AAA03078.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L1L X-ray 1.75 A/B/C/D 1-739 [» ]
ProteinModelPortali Q59490.
SMRi Q59490. Positions 4-724.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK Q59490.

Miscellaneous databases

EvolutionaryTracei Q59490.

Family and domain databases

InterProi IPR000788. RNR_lg_C.
IPR013345. RTP_Rdtase_AdoCbl-dep.
[Graphical view ]
Pfami PF02867. Ribonuc_red_lgC. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02505. RTPR. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiRTPR_LACLE
AccessioniPrimary (citable) accession number: Q59490
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 74 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3