ID   RTPR_LACH4              Reviewed;         744 AA.
AC   A8YW74;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=lhv_0042;
OS   Lactobacillus helveticus (strain DPC 4571).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=405566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPC 4571;
RX   PubMed=17993529; DOI=10.1128/jb.01295-07;
RA   Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA   McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA   Beresford T., Ross R.P.;
RT   "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT   selective gene loss and IS element expansion.";
RL   J. Bacteriol. 190:727-735(2008).
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   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Allosterically regulated by ATP and dNTP.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC       reductase family. {ECO:0000305}.
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DR   EMBL; CP000517; ABX26329.1; -; Genomic_DNA.
DR   RefSeq; WP_012211218.1; NC_010080.1.
DR   AlphaFoldDB; A8YW74; -.
DR   SMR; A8YW74; -.
DR   STRING; 405566.lhv_0042; -.
DR   EnsemblBacteria; ABX26329; ABX26329; lhv_0042.
DR   KEGG; lhe:lhv_0042; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   OMA; FHCNLAE; -.
DR   Proteomes; UP000000790; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:InterPro.
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   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   TIGRFAMs; TIGR02505; RTPR; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Cobalamin; Cobalt; Disulfide bond; DNA replication;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN           1..744
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326542"
FT   REGION          148..159
FT                   /note="Effector region-1"
FT                   /evidence="ECO:0000250"
FT   REGION          169..318
FT                   /note="Effector region-2"
FT                   /evidence="ECO:0000250"
FT   REGION          570..631
FT                   /note="Adenosylcobalamin-binding-1"
FT                   /evidence="ECO:0000250"
FT   REGION          690..729
FT                   /note="Adenosylcobalamin-binding-2"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        413
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000250"
FT   DISULFID        120..424
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   744 AA;  83183 MW;  F4B8613B6264A290 CRC64;
     MPATRITLDS TFIDQVKHEI KPHWGELGWV TYKRTYARWL PEKNRTENWD ETVKRVIEGN
     INLDPRLQDL PSQDVIDKLT NEAQQLFRLV YSLSATPSGR NLWISGTDYQ KRNGDSLNNC
     WFIAIRPQAY GDSHIVPTYI DKRKEAVSMP FSFLFDQLMK GGGVGFSVVD DNINQIPQVD
     HQVDLSVVID KNSKSYDASL KVGAIDKAEW EKNNSGLDNV IYYRIPDTRE GWVLANARLI
     DLHFNDTNPD QKTKLVLDIS DIRPYGAKIH GFGGTASGPM PLVEMFFDIN NVINERVGQK
     LTAVDATDIC NLIGKTVVAG NVRRSAELAL GSSDNQDFIK MKQDKEKLYH HRWASNNSVA
     INSKFNNYGP IADGIMHNGE PGIVNLDLSR NYGRIADGYQ AGIDDDVEGT NPCGEISLAN
     GEPCNLFEVF PYIAEQQGWD LKEAFSLAAR YTKRVTFSHY DWEVSRNIIQ KNRRIGVSMS
     GIQDWLLNDL GHRVVTGFKD ATDKETGAPI KKPIYDPQGI KMVDGLYHAV IAADKAYSEE
     LGVNPSIKHT TVKPSGTVAK LAGVSEGMHF HYAGYLIQRI RFQASDPLLP ALRKCGYHTE
     PDIYTKNTIC VEIPLRAAHA DSKNFASAGT VSIAEQFATQ AFLQTYWSDN AVSCTVTFQA
     NESNQIAPLL HQYRHTIKST SLLPYYGGSL KQAPKEPINK KAYEDRVAMI TGDVKEVFEN
     QNKDQKGLEL VDQSDCTSGA CPIK