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Protein

Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase

Gene

rtpR

Organism
Lactobacillus leichmannii
Status
Reviewed-Annotation score: Annotation score: 5 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)DescriptionActionsGraphical viewLength
Active sitei4081
Active sitei4101

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

BRENDAi1.17.4.2. 2878.
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002214282 – 739Adenosylcobalamin-dependent ribonucleoside-triphosphate reductaseAdd BLAST738

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi119 ↔ 419Redox-active

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1739
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 18Combined sources10
Helixi27 – 32Combined sources6
Turni33 – 35Combined sources3
Turni40 – 43Combined sources4
Helixi48 – 60Combined sources13
Helixi64 – 67Combined sources4
Helixi72 – 90Combined sources19
Beta strandi93 – 96Combined sources4
Helixi98 – 103Combined sources6
Helixi107 – 110Combined sources4
Turni113 – 116Combined sources4
Beta strandi119 – 123Combined sources5
Helixi148 – 158Combined sources11
Beta strandi162 – 166Combined sources5
Helixi169 – 172Combined sources4
Beta strandi183 – 187Combined sources5
Helixi195 – 200Combined sources6
Turni206 – 208Combined sources3
Beta strandi216 – 219Combined sources4
Helixi224 – 236Combined sources13
Helixi240 – 242Combined sources3
Beta strandi249 – 253Combined sources5
Beta strandi267 – 270Combined sources4
Helixi275 – 289Combined sources15
Turni290 – 293Combined sources4
Helixi298 – 313Combined sources16
Beta strandi322 – 327Combined sources6
Helixi331 – 335Combined sources5
Helixi336 – 338Combined sources3
Helixi340 – 345Combined sources6
Helixi347 – 349Combined sources3
Beta strandi350 – 356Combined sources7
Helixi363 – 373Combined sources11
Beta strandi377 – 380Combined sources4
Helixi381 – 386Combined sources6
Helixi390 – 392Combined sources3
Turni396 – 401Combined sources6
Beta strandi402 – 405Combined sources4
Beta strandi411 – 414Combined sources4
Beta strandi421 – 424Combined sources4
Helixi426 – 431Combined sources6
Helixi436 – 450Combined sources15
Helixi458 – 467Combined sources10
Beta strandi471 – 474Combined sources4
Helixi477 – 485Combined sources9
Beta strandi489 – 497Combined sources9
Turni499 – 501Combined sources3
Beta strandi504 – 510Combined sources7
Helixi512 – 536Combined sources25
Beta strandi545 – 547Combined sources3
Helixi551 – 557Combined sources7
Beta strandi569 – 578Combined sources10
Helixi583 – 589Combined sources7
Beta strandi593 – 596Combined sources4
Beta strandi598 – 600Combined sources3
Beta strandi603 – 611Combined sources9
Turni613 – 616Combined sources4
Turni623 – 625Combined sources3
Helixi628 – 641Combined sources14
Beta strandi650 – 653Combined sources4
Helixi655 – 660Combined sources6
Helixi661 – 667Combined sources7
Turni668 – 671Combined sources4
Beta strandi673 – 679Combined sources7
Beta strandi689 – 692Combined sources4
Helixi695 – 704Combined sources10
Helixi709 – 719Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ59490.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni147 – 158Effector region-1Add BLAST12
Regioni168 – 313Effector region-2Add BLAST146
Regioni565 – 626Adenosylcobalamin-binding-1Add BLAST62
Regioni685 – 724Adenosylcobalamin-binding-2Add BLAST40

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)DescriptionActionsGraphical viewLength
Sequence conflicti152F → C in AAA03078 (PubMed:8397403).Curated1
Sequence conflicti717N → D AA sequence (PubMed:8397403).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L1LX-ray1.75A/B/C/D1-739[»]
ProteinModelPortaliQ59490.
SMRiQ59490.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.17.4.2. 2878.
SABIO-RKQ59490.

Miscellaneous databases

EvolutionaryTraceiQ59490.

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.
ProtoNetiSearch...

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 2, 2016
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.