ID   RTPR_NITSB              Reviewed;         650 AA.
AC   A6Q367;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Probable adenosylcobalamin-dependent ribonucleoside-triphosphate reductase;
DE            Short=RTPR;
DE            EC=1.17.4.2;
GN   Name=rtpR; OrderedLocusNames=NIS_0814;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; Nitratiruptor.
OX   NCBI_TaxID=387092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB155-2;
RX   PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA   Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA   Horikoshi K.;
RT   "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT   emergence of pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class II ribonucleoside-triphosphate
CC       reductase family. {ECO:0000305}.
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DR   EMBL; AP009178; BAF69926.1; -; Genomic_DNA.
DR   RefSeq; WP_012082189.1; NC_009662.1.
DR   AlphaFoldDB; A6Q367; -.
DR   SMR; A6Q367; -.
DR   STRING; 387092.NIS_0814; -.
DR   KEGG; nis:NIS_0814; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_002384_0_0_7; -.
DR   InParanoid; A6Q367; -.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000001118; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; -; 3.
DR   InterPro; IPR040763; RNR_alpha_hel.
DR   InterPro; IPR000788; RNR_lg_C.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF17975; RNR_Alpha; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE   3: Inferred from homology;
KW   Cobalamin; Cobalt; Disulfide bond; DNA replication; Oxidoreductase;
KW   Redox-active center; Reference proteome.
FT   CHAIN           1..650
FT                   /note="Probable adenosylcobalamin-dependent ribonucleoside-
FT                   triphosphate reductase"
FT                   /id="PRO_0000326543"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..366
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   650 AA;  74398 MW;  55ED17318FE61465 CRC64;
     MYVEHFFKLP SQTKELLQNT PYRFGFGLLS EVTFYRSYSR LKEDGTNEHW PDTVIRVTEG
     IFSIRKNHAL NYHLPWDEEQ AQIFAKEFAL SMLQLRWLPP GRGLWMMGTR YMYERGSAGL
     YNCAAVDTSN LAHAAEWAMD MLMVGAGVGF NTAWSGKATK PDKKHPKIYV IDDSKEGWVK
     SVRLLIQSYT DNGPFYRFDY SKIRPAGSPL KTFGGIAPGP EPLKRLHKKI EQILDDYLDK
     KIDKTRCVVD LFNNIGLCVV SGNIRRSAEI AIGRPGDKTF LHLKDYEKFP ERKEYGWISN
     NSVVIENLDD FHYIDAITSL IASNGEPGVL HLENMQKYGR FGEIVPDRAW LSNPCGEIAL
     ESYELCNLSE IFISKCSNEE DFQKLIEYAT FYASTVNLLP THRPETNEII ARNRRIGVSV
     SGVADAIEKF GLETIIKWLR KGYEKVRTVN ERLAKEAGIP VSLKVTCVKP SGTISILAGT
     SPGMHYPLAT YALRRIRIGK TSKLAKLLID SGLSFEEDIY DKNSYVFAFP IHYDNPRSIK
     EVDIYEQMLV LTMLQREWAD NMVSNTIQFD PTRYDAKDLS QIVKHFLPMI KSLTLLPEKE
     TIYPQMPFES IKKEEFEKRV TQLPKVEWNT LSGHHADSER FCSTQSCQID
//