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Q59490

- RTPR_LACLE

UniProt

Q59490 - RTPR_LACLE

Protein

Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase

Gene

rtpR

Organism
Lactobacillus leichmannii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Adenosylcobalamin.

    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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    MSEEISLSAE FIDRVKASVK PHWGKLGWVT YKRTYARWLP EKGRSENWDE    50
    TVKRVVEGNI NLDPRLQDSP SLELKQSLTE EAERLYKLIY GLGATPSGRN 100
    LWISGTDYQR RTGDSLNNCW FVAIRPQKYG DSKIVPSYLG KQEKAVSMPF 150
    SFLFDELMKG GGVGFSVARS NISQIPRVDF AIDLQLVVDE TSESYDASVK 200
    VGAVGKNELV QDADSIYYRL PDTREGWVLA NALLIDLHFA QTNPDRKQKL 250
    ILDLSDIRPY GAEIHGFGGT ASGPMPLISM LLDVNEVLNN KAGGRLTAVD 300
    AADICNLIGK AVVAGNVRRS AELALGSNDD QDFISMKQDQ EKLMHHRWAS 350
    NNSVAVDSAF SGYQPIAAGI RENGEPGIVN LDLSKNYGRI VDGYQAGIDG 400
    DVEGTNPCGE ISLANGEPCN LFEVFPLIAE EQGWDLQEVF ALAARYAKRV 450
    TFSPYDWEIS REIIQKNRRI GISMSGIQDW LLTRLGNRVV TGFKDDFDPE 500
    THEAIKVPVY DKRAIKMVDQ LYKAVVKADQ DYSKTLGCNE SIKHTTVKPS 550
    GTVAKLAGAS EGMHFHYGAY LIQRIRFQDS DPLLPALKAC GYRTEADIYT 600
    ENTTCVEFPI KAVGADNPNF ASAGTVSIAE QFATQAFLQT YWSDNAVSCT 650
    ITFQDSEGDQ VESLLRQYRF ITKSTSLLPY FGGSLQQAPK EPIDKETYEK 700
    RSQEITGNVE EVFSQLNSDV KDLELVDQTD CEGGACPIK 739
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20047 Unassigned DNA. Translation: AAA03078.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20047 Unassigned DNA. Translation: AAA03078.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 73 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