ID A0A0G0AXU6_9BACT Unreviewed; 1136 AA.
AC A0A0G0AXU6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=UR56_C0007G0021 {ECO:0000313|EMBL:KKP62038.1};
OS Candidatus Roizmanbacteria bacterium GW2011_GWC2_34_23.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1618484 {ECO:0000313|EMBL:KKP62038.1, ECO:0000313|Proteomes:UP000034004};
RN [1] {ECO:0000313|EMBL:KKP62038.1, ECO:0000313|Proteomes:UP000034004}
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:KKP62038.1}.
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DR EMBL; LBPR01000007; KKP62038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0AXU6; -.
DR STRING; 1618484.UR56_C0007G0021; -.
DR PATRIC; fig|1618484.3.peg.315; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034004; 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; 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; 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 397..541
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 630..652
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 1136 AA; 127391 MW; CBA24129F661C317 CRC64;
MKLKGISEKV FLDRYSLKNK EGKAMEKRPE EMWARIAKAV SVVEKKSKQK KWEKEFYSAL
KDFKYVPGGR ILSGAGTGYD VSFYNCFVIP SPEDSRGGIL KTLGQMVEIM ARGGGVGINL
SSLRPRGARV KKVNGFSSGP INWAELFSVA TRDIIQQGGT RRGALMLMLW DWHPDIEEFI
TVKQDLSKIN GANLSLCVSD TFMEAVEKDS DWPLVFPDIK DPEYDRKWTG DLDAWKKMGK
KVIVHKIVKA RKLWDLVASA AWKSAEPGVV FMERYNKLYN NYYWNKIICV NPCVTGDTLV
NTTNGLITMK KLYEKRLPFR VVVNGKDYLS TAVKLTGKKQ IYRLITKEGY QLRLTADHKV
FTPFGKKSAG ELKKGEKIIL ATGGYFGTKG TLDEGRVLGW LVGDGSIKKD VVTLYFYQKE
KQELAPRFAL MVEKMVEGEQ VVARPYHIAP QYIEKENKTV IESVRLWRIA YRYGLSHENK
YQVPEAIFAG SEGIQRGFLQ GIFSSDGTVI GTIEKGVSIR LTSIKKSLLI SVQRLLLNFG
IFSKIYENRR QEGKRFLPDG RGGLKLYNCQ AYHELVISKE NLIKFSGLVG FLQQEKQNKL
QSFLSLYRRG PYKEKPEATF LKLEKEEIEE VFDITVEGIH GFSANGLLVS NCGEEGLPPW
GVCNLGSINL SALVKGKDID EKGKFDFNAL KNIVRIAVRF QDNVVDMDPY IFEGIRKTQL
EGERRIGLGT MGLGDTLIKL HLRYGSPESL EFIDYAREKG SFVKYDRKLY LEGKFVDQLP
DDVKKSIKKN GIRNSLLLMQ APTGSTSLMA GTTSGIEPVY EFEFIRKDRI GTHIIRHDLY
DSWFKKHSKE VEAEKVKKPE WFVSANELTP EDHVKVQGVI QKYVDASISK TVNAPTSHTV
EDVKKLYNLA YKLGCKGIAY MRDGSRPGVL ERKPEPAEAK TSKQVVCPPP SYTIKPRPMV
VHGATYRINT PVGIAFITLN TNGGNPPEPL EIFINVGKAG SDVYAMAEGL GRMISVALRF
SSHISVFDRV NEIITQLQGI GGARTMGFGK DRIRSLPDAV AKVLSMHYGM NGEEKPNGVV
KEDPKLVTAT TQPSLIQPAV AVARSTSFDI CPSCGEVTLV HEEGCKKCYG CGYSEC
//
