ID A0A1J5B7U4_9BACT Unreviewed; 960 AA.
AC A0A1J5B7U4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=AUK18_02060 {ECO:0000313|EMBL:OIP03415.1};
OS Candidatus Beckwithbacteria bacterium CG2_30_44_31.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1805035 {ECO:0000313|EMBL:OIP03415.1, ECO:0000313|Proteomes:UP000183605};
RN [1] {ECO:0000313|EMBL:OIP03415.1, ECO:0000313|Proteomes:UP000183605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_44_31 {ECO:0000313|EMBL:OIP03415.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP03415.1}.
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DR EMBL; MNXQ01000038; OIP03415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5B7U4; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000183605; 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; 2.
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; 2.
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 413..550
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 620..642
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 960 AA; 108570 MW; 13D0385F6E5E244A CRC64;
MKIIQPRQSP IALEITRKRY LMADSKGRIM ETVGEMLWRV AKHIAKFEED KKVAEAFYER
MVTKKFVCSG KAMFEAGSPG GCGQLAACFV LPIEDSIDSI FKTLGEAAVI HKNNGGTGFN
FSKIRPHGDK VKNVPHAASG PVDFIKAFSA ALSKILQGAK RQGANIAILN ADHPDIEEFI
RMKTEDGTIK NFNISVGASD EFMKAVRLKK IWQLVNPRNK EAVKKIRADK LFDLICEYAW
KTADPGMAFL DRLDRDNPTP TLGKIEATNP CITGDALVST KHGLMEFAKI YEHYHNPGRM
GLLVDQRVVG NQGMAIKQSL QVLCQGVKQV FELETKSGFH LKATGNHKVM TETGWKELVQ
IKPGERVLIQ ASAGQFSQNK HLPFEWNNKL TGRNGRKYHL SLPTRWSKEL GVFLGWLVGD
GFVRKKYAIL AFGSKKLAEQ KYFARLLQRW YPSTMIRQPT ERTTQVVCHS QFVADYAMQF
GVLAVKSAEK RVPKTIFTAP KETVIGFLQG LFGADGTIGF VKDKSSYMRL SSKSRLLLTD
VQLLLLNLGI KARIYNRSRP PRRKLWELEI SKDGVIKFLD EVGFLFDRHE EKIKKLRGKS
YYSTRFSDEV LVVTPLGKEA VYDVVEPETH SFIANGFIVH NCGEIGLLPY ESCNLGSINL
SEHVKNEKRK TKNEKLEIDW EELRKTIRIG VRFLDNMIEV NNYPLEQVKR IVKDGNRRIG
LGVMGLAHLF YKLQIPYNSE KAVKLSEKLA QFIRIEADKE SERLGRERGN FGNYDVSIYA
KSGKARRNCA TTMIAPTGTI SMFADCSSGI EPVFALTTTR RTFFEDSRKN SSTKEVIVND
PVYQEYKDRY EQKVFVTAHE IGWRWHVKIQ AAWQKYFDNS VSKTINFPKE ATVEEVKQAY
LLAWKLGCKG MTIYRDGSKQ DQVLNNPASA GQVCPECGYE LIIKEGCSSC LNCGYSKCSL
//
