ID   RTPR_LACDA              Reviewed;         739 AA.
AC   Q1G7W2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=Ldb0096;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC   NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(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; CR954253; CAI96937.1; -; Genomic_DNA.
DR   RefSeq; WP_003622993.1; NZ_JQAV01000017.1.
DR   AlphaFoldDB; Q1G7W2; -.
DR   SMR; Q1G7W2; -.
DR   STRING; 390333.Ldb0096; -.
DR   KEGG; ldb:Ldb0096; -.
DR   PATRIC; fig|390333.13.peg.812; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   BioCyc; LDEL390333:LDB_RS00375-MONOMER; -.
DR   Proteomes; UP000001259; 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   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; Reference proteome.
FT   CHAIN           1..739
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326539"
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;  81910 MW;  AA7CFEDC22FC74CF CRC64;
     MSEGISLSAE FIDRVKASVK PHWGKLGWVT YKRTYARWLP EKGRSENWDE TVKRVVEGNI
     NLDPRLQDSP SLELKQSLTE EAERLYKLIY GLGATPSGRN LWISGTDYQR RTGDSLNNCW
     FVAIRPQKYG DSKIVPSYLG KQEKAVSMPF SFLFDELMKG GGVGFSVARS NISQIPRVDF
     AIDLQVVVDE SSESYDASVK VGAVGKNELV 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
//