ID   RTPR_LEVBA              Reviewed;         749 AA.
AC   Q03PB4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=LVIS_1898;
OS   Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS   1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=387344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC   947 / NCTC 947;
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; CP000416; ABJ64958.1; -; Genomic_DNA.
DR   RefSeq; WP_011668579.1; NC_008497.1.
DR   AlphaFoldDB; Q03PB4; -.
DR   SMR; Q03PB4; -.
DR   STRING; 387344.LVIS_1898; -.
DR   PRIDE; Q03PB4; -.
DR   EnsemblBacteria; ABJ64958; ABJ64958; LVIS_1898.
DR   KEGG; lbr:LVIS_1898; -.
DR   PATRIC; fig|387344.15.peg.1805; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_002384_0_0_9; -.
DR   OMA; FHCNLAE; -.
DR   OrthoDB; 357568at2; -.
DR   Proteomes; UP000001652; 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; Reference proteome.
FT   CHAIN           1..749
FT                   /note="Adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326537"
FT   REGION          152..163
FT                   /note="Effector region-1"
FT                   /evidence="ECO:0000250"
FT   REGION          173..321
FT                   /note="Effector region-2"
FT                   /evidence="ECO:0000250"
FT   REGION          573..634
FT                   /note="Adenosylcobalamin-binding-1"
FT                   /evidence="ECO:0000250"
FT   REGION          693..734
FT                   /note="Adenosylcobalamin-binding-2"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..427
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   749 AA;  82998 MW;  BA3CE5E18509931F CRC64;
     MNTATQASVS LTPEFIAATE KEITPHWGEL GWVTYKRTYA RWLPEQQRNE EWPETVKRVV
     EGNINLDPRL QADTVTPEVL TELTTEAQNL FRLIYGLAAT PSGRNLWISG TDYQHRNGDA
     LNNCWFIAVR PQAYGDSHIL PSYLTQDQVA VSMPFSFMFD QLMKGGGVGF SVTPNNVHQM
     PVVDQTVDLT IVIDPESASY ADSVALGAVN RSEWMHDNSL ADVRFYRLPD TREGWVLANA
     NMMDAHFNST NPEKKTKVVL DISDIRPKNA PIHGFGGTAS GPMPLVEMLF DINQILNNAV
     GRQLTAVDCT DMGNMIGKTV VAGNVRRSAE LALGGAEDDA FITMKQDKDQ LYHHRWASNN
     SVAVDSDFTD YAPIADSIQH NGEPGIVNLG LSRNYGRLID GRQEGIDEAV EGTNPCGEIS
     LSNGEPCNLF EVFPSVAEEQ GWQLEDAFGL GARYTKRVTF SHYDWEVSRK AIQKNRRIGV
     SMSGIQDWIL KTFKQRVVTG FEAKHDAETG KTFMQPIYNQ AAVNRFNALY QAVVKADQDY
     SDTLGCQPSI KHTTVKPSGT VAKLAGVSEG MHFHYARYLI QRIRFQDSDP LLPALKASGY
     KVEPDVYSQN TMCVEFPVKA AHADEPAFAS AGEVSMAEQF ATQAFLQTYW SDNAVSCTVT
     FQPEEGQDIS DLLLQYRHTI KSTSLLPYSG ADFKQAPKEP IDAATYDAKC QEITADVAEK
     FAAMTGNHDQ KDIELVDQSD CESGACPIR