ID   RTPR_LACP3              Reviewed;         748 AA.
AC   Q035U1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=LSEI_2287;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 /
RC   NRRL B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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   -!- 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; CP000423; ABJ71031.1; -; Genomic_DNA.
DR   RefSeq; WP_011674848.1; NC_008526.1.
DR   RefSeq; YP_807473.1; NC_008526.1.
DR   AlphaFoldDB; Q035U1; -.
DR   SMR; Q035U1; -.
DR   STRING; 321967.LSEI_2287; -.
DR   PaxDb; 321967-LSEI_2287; -.
DR   KEGG; lca:LSEI_2287; -.
DR   PATRIC; fig|321967.11.peg.2250; -.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   Proteomes; UP000001651; 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   Gene3D; 3.20.70.20; -; 1.
DR   Gene3D; 3.30.1620.10; b-12 dependent (class ii) ribonucleotide reductase, Chain A, Domain 2; 1.
DR   Gene3D; 3.90.1390.10; b-12 dependent (class ii) ribonucleotide reductase, chain A, domain 3; 1.
DR   InterPro; IPR040763; RNR_alpha_hel.
DR   InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
DR   NCBIfam; TIGR02505; RTPR; 1.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Cobalamin; Cobalt; Disulfide bond; DNA replication;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..748
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326538"
FT   REGION          151..162
FT                   /note="Effector region-1"
FT                   /evidence="ECO:0000250"
FT   REGION          172..320
FT                   /note="Effector region-2"
FT                   /evidence="ECO:0000250"
FT   REGION          572..633
FT                   /note="Adenosylcobalamin-binding-1"
FT                   /evidence="ECO:0000250"
FT   REGION          692..733
FT                   /note="Adenosylcobalamin-binding-2"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        415
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..426
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   748 AA;  82300 MW;  48F280F385F1DC75 CRC64;
     MQVMTKPITL APAFIAEVKK EIKPHWGELG WVTYKRTYAR WLPDAQRTEN WDETVKRVVE
     GNINLDPRLH TANPDPKVVE TLQKEARNLF KLIYGLAGTP SGRNLWISGT DYQKRNGDAL
     NNCWFIAIRP QPYGQSHIVP EDYPASQPAV SMPYSFMFDE LMKGGGVGFS VTKDNIAKLP
     PVATKLELTV VIGRNSASYA DSLKMGAVDR DEWEKAHAGE QADHCALPDT REGWVLANAK
     VIDHHFAATN PSGQTKLVLD ITNIRPKGAR IHGFGGTASG PMPLIEMLLD INKLLNARVG
     QHLTAVDATD IGNLIGKTVV AGNVRRSAEM SLGSADDEDF ITMKQDQKQL YHHRWASNNS
     VAINTQFDAY SPIALAIAKN GEPGIVNLEL SRRFGRIADR ENAENDPDVE GTNPCGEISL
     ANGEPCNLFE VFPVVAVEQG WKLKQAFTLA ARFAKRVTFS HYDWQVSRDI IKKNRRIGVS
     MSGIQDWFLN DFGRRVVSGF ESVVDPQTGK MVQKPIYDPE IKQAVDGLYH TVVDADQAYS
     DALGCEPSRK HTTVKPSGTV AKLAGVSEGM HFHYAGYLIQ RIRFQGNDPL LPALQACGYH
     IEPDVYTKGT MVVEFPIRAA HADDPAFASA GTVSIAEQIA TQAFLQTYWS DNAVSCTVTF
     QPKEADQIAG LLSQYRHVIK STSMLPYVGA GFKQAPKEPI DVKTYKQKCA AIHGSVAAVF
     AVQNADHDQK DLELVDQTDC AGGACPIK
//