ID   RTPR_EUGGR              Reviewed;         729 AA.
AC   Q2PDF6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rnr;
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP   COFACTOR, AND SUBUNIT.
RC   STRAIN=SAG 1224-5/25;
RX   PubMed=16368684; DOI=10.1074/jbc.m512962200;
RA   Torrents E., Trevisiol C., Rotte C., Hellman U., Martin W., Reichard P.;
RT   "Euglena gracilis ribonucleotide reductase: the eukaryote class II enzyme
RT   and the possible antiquity of eukaryote B12 dependence.";
RL   J. Biol. Chem. 281:5604-5611(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         triphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         triphosphate; Xref=Rhea:RHEA:12701, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.17.4.2;
CC         Evidence={ECO:0000269|PubMed:16368684};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000269|PubMed:16368684};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16368684}.
CC   -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC       reductase family. {ECO:0000305}.
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DR   EMBL; AJ620503; CAF05662.1; -; mRNA.
DR   AlphaFoldDB; Q2PDF6; -.
DR   SMR; Q2PDF6; -.
DR   SABIO-RK; Q2PDF6; -.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR040763; RNR_alpha_hel.
DR   Pfam; PF17975; RNR_Alpha; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Cobalamin; Cobalt; Direct protein sequencing;
KW   Disulfide bond; DNA replication; Oxidoreductase; Redox-active center.
FT   CHAIN           1..729
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326545"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..438
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   729 AA;  82175 MW;  91F4F84D8B2E297C CRC64;
     MAEKENVHPQ VISSFPTPSK ALKLSEKSSL KDVQTDNAAV PLVVDETSYP EPTCEFYGGL
     LGPQLPEAER FVLDPALVEE YRHKKPPFGF NGLGEVVYLR TYAREKDNGQ SEVWLDTVQR
     VVTGTFEVLQ HHVVNKLHCH WDAQKAKERS EDMFRRIFEM KFLPPGRGLW AMGSPICRKK
     GFAAALNNCA FVSTATLEKD RVGPFLFLMD ASMLGVGVGF DNAGAGSFTV PGPDDTQPTY
     KFMIPDKREG WVESLKRLLK AHFCHTADVE FDYSKIREMG TKLKTFGGTS SGPGPLINLH
     KSIRKILVGE KGKPISVTCI TDIMNLIGVC TVAGNIRRSA EIAFGEADCK EFLDLKSYET
     NPHRVEYGWA SNNSIFAKVG MDYSDACERV RTNGEPGFAW LSNMQAFSRM NGKPDYRDQR
     VLGGNPCLEQ SLESMELCCL VETFPDKHET LEDFKRTLYS ALLYAKTVTL LPLHWRESNE
     IMLRNRRIGC SVSGIAQFIT NRGLHELKTW LEEGYDILHQ YDCQISEWLC IRQSIKLTSV
     KPSGTISLVA GATPGVHYPE SCYYTRRLRM ARDSPLLERL IKAGYHVEPC CVAPDVTAIV
     EFPVAAGNSI RTTRDITMWE QLSLAAFMQR YWADNQVSAT ITFDPETEGL HLNQALQYFQ
     YQLKGISFLP RYPMGAFKQM PYEAITKEQY EEAIRKVKED VSLSSANAIA ETVEENQQTF
     CDNDRCIKL