RTPR_LACP3
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 03-AUG-2022, entry version 89.
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; Firmicutes; 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 / NRRL
RC 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 EnsemblBacteria; ABJ71031; ABJ71031; LSEI_2287.
DR KEGG; lca:LSEI_2287; -.
DR PATRIC; fig|321967.11.peg.2250; -.
DR HOGENOM; CLU_002384_0_0_9; -.
DR OMA; FHCNLAE; -.
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 InterPro; IPR040763; RNR_alpha_hel.
DR InterPro; IPR013345; RTP_Rdtase_AdoCbl-dep.
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..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
