ID   RTPR_LACDB              Reviewed;         739 AA.
AC   Q04CQ7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=LBUL_0079;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365 / Lb-18).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-365 / Lb-18;
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; CP000412; ABJ57765.1; -; Genomic_DNA.
DR   RefSeq; WP_003620293.1; NC_008529.1.
DR   AlphaFoldDB; Q04CQ7; -.
DR   SMR; Q04CQ7; -.
DR   KEGG; lbu:LBUL_0079; -.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   BioCyc; LDEL321956:LBUL_RS00360-MONOMER; -.
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   CDD; cd01676; RNR_II_monomer; 1.
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.
FT   CHAIN           1..739
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326540"
FT   REGION          147..158
FT                   /note="Effector region-1"
FT                   /evidence="ECO:0000250"
FT   REGION          168..313
FT                   /note="Effector region-2"
FT                   /evidence="ECO:0000250"
FT   REGION          565..626
FT                   /note="Adenosylcobalamin-binding-1"
FT                   /evidence="ECO:0000250"
FT   REGION          685..724
FT                   /note="Adenosylcobalamin-binding-2"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..419
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   739 AA;  81896 MW;  AA7CF94DD05214CF CRC64;
     MSEGISLSAE FIDRVKASVK PHWGKLGWVT YKRTYARWLP EKGRSENWDE TVKRVVEGNI
     NLDPRLQDSP SLELKQSLTE EAERLYKLIY GLGATPSGRN LWISGTDYQR RTGDSLNNCW
     FVAIRPQKYG DSKIVPSYLG KQEKAVSMPF SFLFDELMKG GGVGFSVARS NISQIPRVDF
     AIDLQVVVDE SSESYDASVK VGAVGKNEVV QDADSIYYRL PDTREGWVLA NALLIDLHFA
     QTNPDRKQKL ILDLSDIRPY GAEIHGFGGT ASGPMPLISM LLDINEVLNN KAGGRLTSVD
     AADICNLIGK AVVAGNVRRS AELALGSNDD QDFISMKQDQ EKLMHHRWAS NNSVAVDSAF
     SGYQPIAAGI RENGEPGIVN LDLSKNYGRI VDGYQAGIDG DVEGTNPCGE ISLANGEPCN
     LFEVFPLIAE EQGWDLQEVF ALAARYAKRV TFSPYDWEIS REIIQKNRRI GISMSGIQDW
     LLTRLGNRVV TGFKDDFDPE THEAIKVPVY DKRAIKMVDQ LYKAVVKADQ DYSKTLGCNE
     SIKHTTVKPS GTVAKLAGAS EGMHFHYGAY LIQRIRFQNS DPLLPALKAC GYRTEADIYT
     ENTTCVEFPV KAVGADNPNF ASAGTVSIAE QFATQAFLQT YWSDNAVSCT ITFQDSEGDQ
     VESLLRQYRF IIKSTSLLPY FGGSLQQAPK EPIDKETYEK RSQEITGNVE EVFSQLNSDV
     KDLELVDQTD CEGGACPIK
//