ID A0A0G1CQD9_9BACT Unreviewed; 1169 AA.
AC A0A0G1CQD9;
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=UV61_C0001G0069 {ECO:0000313|EMBL:KKS87662.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWB1_43_11.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618446 {ECO:0000313|EMBL:KKS87662.1, ECO:0000313|Proteomes:UP000034050};
RN [1] {ECO:0000313|EMBL:KKS87662.1, ECO:0000313|Proteomes:UP000034050}
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:KKS87662.1}.
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DR EMBL; LCFD01000001; KKS87662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1CQD9; -.
DR STRING; 1618446.UV61_C0001G0069; -.
DR PATRIC; fig|1618446.3.peg.75; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034050; 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; 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; 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 398..542
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 631..653
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
SQ SEQUENCE 1169 AA; 129638 MW; 917C72DB18DF02E1 CRC64;
MQLTGIRSKV FLDRYALKDK EGKPIEQTPE EMWRRIARGV ADNEKTVKEK KYWENEFYEA
MTDFKFVPGG RILSGAGTGY KVTYYNCFVI PSPKDSRGGI LETLKQMVEI MARGGGVGIN
LSSLRPRGAR VKKVNGFSSG PCNWAELFSV ATKDIIQQGG TRRGALMLML WDWHPDVEEF
ITVKQDLSRI NGANLSVCVS DSFMEAVKND RDWDLVFPDK DDPDYDTKWD GIMQHWLDLG
KKPKVVKTIK ARSLWDLICQ AAWRSAEPGL VFMERYNKQH SNYYFNYINC VNPCVTGDTL
VATSDGLKYM RQLYEENTPF TAIVNGKAYL STAVKKTGVK PVFRLKTHEG YELRLTRDHK
VVTLDGPKAA EKLTPSDKIV LTSGGGFGKN GSLEEGQVLG WLVGDGSMKK DVATLYFYHD
EKKELAPKFA TMVSQLVAGE QVVARSYSVT PQYVEKENKA VVESVRLWRI AQRYGLTHAN
EYLVPKAVLA GSEMMQRGYL QGLFSSDGHV AGTPEKGVSA RLTSISKALL VDVQRLLLNF
GIMSRIYENR RADGIRKLPN GKGAYADYHC QAYHDLVISK SDLVTFAGLI GFLQKAKQEK
LRSLLSRYTR GPYRQQLVAT VKELEPDGIE EVFDITVSEI HQFSANGLLV LNCGEEGLPA
WGVCNLSSIN LAALVNEKGE MDYKLLAKIA KISVRFQDNI IDQDVYVFPG IRETQLNGER
RIGLGTMGLG DALIKMGIRY GSEESIVVCD KIYKIIRDAA FEASVETARD KKPFPKFNAE
KYLKGYFIKQ LPEHIRAGIK KQGIRNSVLL MQAPTGSTSL LSGTSSGIEP VYEFEFIRRD
RLGEHILRHP LYDAWFADFK AKNGRNPKPE ERPSYFVSAN DLTPEDHVKV QAVIQKYVDA
SISKTVNAPN AHTVEDVKKL YMMAYDLGCK GVTYMRDGSR AGVLERITEK KAETVQTLPA
QAGNGHTALT PTPIQPEIKP RPMVVHGSTY KIETPVGKAY VTVNSNGEGR ENPFEVFVTV
GKAGSDVAAM ADGIGRLISL VLRMASPLSE KERVKQVIHQ LGGIGGSRHV GFGEKRVRSL
PDAISKVLGE HIKSTNGQAT LSTNGHGVVG NGHAETQIET EPVVPAVVAG QQPLFAKPVE
FDLCPSCGEA LLAHEEGCKK CYGCGYSEC
//
