ID   RTPR_LACAC              Reviewed;         744 AA.
AC   Q5FMX8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, 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=LBA0041;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV41946.1; -; Genomic_DNA.
DR   RefSeq; WP_003549289.1; NC_006814.3.
DR   RefSeq; YP_192977.1; NC_006814.3.
DR   AlphaFoldDB; Q5FMX8; -.
DR   SMR; Q5FMX8; -.
DR   STRING; 272621.LBA0041; -.
DR   GeneID; 56941656; -.
DR   KEGG; lac:LBA0041; -.
DR   PATRIC; fig|272621.13.peg.39; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   OrthoDB; 9763270at2; -.
DR   BioCyc; LACI272621:G1G49-39-MONOMER; -.
DR   Proteomes; UP000006381; 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..744
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326536"
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;  83521 MW;  4D3564C885BB1EB0 CRC64;
     MSSTRIELDQ DFIDQVKHEI KPHWGELGWV TYKRTYARWL PEKNRSENWD ETVKRVIEGN
     VNLDPRLQGT PSEEVINELT NEAKQLFRLT YGLSATPSGR NLWISGTDYQ KRTGDSLNNC
     WFIAIRPQEY GDSHIVPTYI DKREKAVSMP FSFLFDQLMK GGGVGFSVVN SNIKQIPKVD
     NKIDLTVVIN KSSKSHDASI KVGAVDKDEW EKQNPDHDDI IYYRLPDTRE GWVLANARLI
     DMHFNNTNPD QKTKLVLDIS DIRPYGAKIH GFGGTASGPM PLVEMFIDIN NVINARVGKN
     LTAVDATDIC NLIGKTVVAG NVRRSAELAL GSNDDQDFIK MKQDKEKLYH HRWASNNSVA
     INSKFNNYGP IADGILHNGE PGIVNLDLSR NYGRIVDGYQ PGIDDDVEGT NPCGEISLAN
     GEPCNLFEVF PYTAEKQGWN LKEAFTLATR FAKRVTFSHY DWEVSRKIIQ KNRRIGVSMS
     GIQDWLLNDL GHRVVTGFED AVDEQSGEKI KKPIYDPKGI EMVDSLYKAV ITADKAYSEE
     LGVNPSIKHT TVKPSGTVAK LAGVSEGMHF HYAGYLIQRI RFQASDPLLP ALKECGYHTE
     PDIYTKNTIC VEFPLRAAHA DSKNFASAGT VSIEEQFATQ AFLQTYWSDN AVSCTITFQS
     DENDEIAPLL RQYRHTIKST SLLPYYGGSL KQAPKEPINK KTYEERAALI TDDVEEVFTK
     QNDDQKGLEL VGQTDCEGGA CPIK
//