ID A0A0G0HXE0_9BACT Unreviewed; 1173 AA.
AC A0A0G0HXE0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=US31_C0028G0004 {ECO:0000313|EMBL:KKQ16689.1};
OS Berkelbacteria bacterium GW2011_GWA1_36_9.
OC Bacteria; Candidatus Berkelbacteria.
OX NCBI_TaxID=1618331 {ECO:0000313|EMBL:KKQ16689.1, ECO:0000313|Proteomes:UP000034508};
RN [1] {ECO:0000313|EMBL:KKQ16689.1, ECO:0000313|Proteomes:UP000034508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKQ16689.1}.
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; LBSM01000028; KKQ16689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0HXE0; -.
DR PATRIC; fig|1618331.3.peg.935; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034508; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000}.
FT DOMAIN 441..584
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 672..694
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 1173 AA; 129989 MW; 974CDBA8DEFA36EE CRC64;
MSQKTSLLDE VQPKIVKLEL SENALRVIAK RYLMKDRNLE PIETPEEMFQ RVAKHIAKED
SNYGATKEEI SKTENQFYNV MASLEFLPNS PTFTGAGTKL GQLSACFVLP IEDDMKSILK
TQMDMGLIHK SGGGTGFSFS RLRPKNDAVG STGGISSGPI GFLQMYNDTT ECIKQGGTRR
GANMGILRID HPDILEFISY KEKEGTLINF NISIALTKDF MKALEKDEEY ELINPRDGNH
TGKLKAREVF DKIVDGAWRN GEPGIIFLDK INEKNPTPKV GEIEATNPCV TGETLVSTEK
GLMRIDTIAS IYSDGGLNIV TDEVVSENTG YDYYSSGGTA LATTTKIKRR CSLNTISRAF
KTGIKPVYHL TTESGYEITA TADHKIYTQD GWVLLQNIQP GYHTVYLQSQ AGAFNISNNL
PSTTVHKLSL PTKWSKELGE IMGLIVGDGW LIKSGKNCRL GLTFGESNED VLNYIKPIMN
GFYGKNIKEI ARPNGTYHLS YHGKFLIEFF SQLGISSNKA ASKKVPETIF TAPKEAVIGF
LRGLFSADGT IAWHEKNQNK YIRLTSKSLA LVKGVQVLLL NLGIKSKIYN RSRDARWGFP
YTNKNGQSKK YLLDGILYEL NISKSSLKVF LNQIGFINQK HSILSQKLLK LNCRNEKWEE
TAKEVKSIGL KEVYDLTEPS THSFIANGIV ISNCGEQPLL PYESCNLGAL NLKKFTKVES
GQTEVDWNKL EKVISDAVHF MDNVIDINKY PVAEIEKMTK LNRKIGITVM GFADMLYNLG
IPYDSDEGLK MAEKIMGFIE KKSHEASQKI AKTRGEFPNF PESVWSKNNG PKMRHAATTS
CNPTGTLSII GTCSSGIEPF FALAYTKTVM DGTALQEVNE HFLRVAKQRG FYNQELLEKI
LETGSIQEID SVPQDVKKVF KVASDIAPEW HVKMQAAFQK HTDGAISKTI NFPNSATRED
VEKAYLLAYK LNCKGLTVYR DGSRNAQVLT VGTSTPTPTI TATSETKITP RERPDIIHGS
TYRIKTAYGK LFITINDDEN GTPFEVFSHL GKAGGFFAAK AEAICRLISL ALRSGVDPEE
IIDQLKGIRG PTPTWSEDGK MILSMPDAIS QILEKHITKS QAHLDLDFKP AEQLKPLSLA
DLGEAPACPE CGALLEISEG CLKCNLCGFS KCG
//
