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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
