ID   RTPR_LACGA              Reviewed;         744 AA.
AC   Q041L3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   13-SEP-2023, entry version 90.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=LGAS_1503;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS   102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 /
RC   KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ60859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000413; ABJ60859.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_021314961.1; NZ_WBMG01000003.1.
DR   AlphaFoldDB; Q041L3; -.
DR   SMR; Q041L3; -.
DR   GeneID; 69665946; -.
DR   KEGG; lga:LGAS_1503; -.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   BioCyc; LGAS324831:G1G6Y-1498-MONOMER; -.
DR   Proteomes; UP000000664; 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.
FT   CHAIN           1..744
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326541"
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;  83638 MW;  FB8C507078BC8CED CRC64;
     MSDLRITLDP DFIAQTKKEV TPHWGELGWV TYKRTYARWL DDKNRSENWD ETVKRVIEGN
     INLDPRLKNN PSKKTIHELT AEAKQLFRLV YGLAATPSGR NLWISGTDYQ KRNGDSLNNC
     WFISIRPQKY GNSHIVPAYL TQDQVAPSMP FSFLFDQLMK GGGVGFSVVD ENINQIPKLD
     QKVDLTIVID KQSKSYDASL KLGATDLDEW KKTNQEKEDY IYYKLPDTRE GWVLANARLI
     DMHFNSTNPE NKKKLVLDIS DIRPYGAKIH GFGGTASGPM PLIEMLFDIN QILNERAGQK
     LTAVDATDIC NLIGKTVVAG NVRRSAELAL GSSNNQDFIT MKQDKKKLYH HRWASNNSVA
     INSEFDNYQP IADSILHNGE PGVVNLELSR NYGRIKDGYQ AGIDGEVEGT NPCGEISLAN
     GEPCNLFEVF PFIAQKQGWD LKEAFKLAAR YTKRVTFSPY DWEVSRKIIN KNRRIGVSMS
     GIQDWILSTF GHRVVTGFKT ATDSETGKEI KDPVYDPEII KTVDGLYQAV VDADKDYSQE
     LNCNTSIKHT TVKPSGTVAK LAGVSEGMHF HYSGYLIQRI RFQETDPLLP ALKDCGYRTE
     PDIYTPHTIC VEFPIKAANA DSDNFASAGT VSIAEQFATQ AFLQTYWSDN AVSCTITFQN
     DESDQIAPLL HQYRYAIKST SLLPYYGGSL KQAPKEPISK EKYEKADNHI TGNVEIVFEQ
     TNEDQKGLEL VDQSDCDNGA CPIK
//