ID A0A0G0PZ43_9BACT Unreviewed; 880 AA.
AC A0A0G0PZ43;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=UT61_C0008G0027 {ECO:0000313|EMBL:KKR30371.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA1_39_8.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618552 {ECO:0000313|EMBL:KKR30371.1, ECO:0000313|Proteomes:UP000034793};
RN [1] {ECO:0000313|EMBL:KKR30371.1, ECO:0000313|Proteomes:UP000034793}
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: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
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:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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:KKR30371.1}.
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DR EMBL; LBXL01000008; KKR30371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0PZ43; -.
DR PATRIC; fig|1618552.3.peg.330; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034793; 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: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:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 56..136
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 140..465
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 469..617
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 880 AA; 96567 MW; 6AF12EA76766E9DB CRC64;
MTSKLKNRKT SKSVDNEKLA LDSLFFPSYE EVTNEIRKKL GKRPHLPKGL PKGDWTEQSL
KVLAERYLRK NDDGELIETP EEMCWRVAWD VASAEIRWGA KKRDVLRSAK EFYNLLITHE
FLPNSPTLMN AGTGNGLQYS ACFVLPVEDS LVGIFDAIKH QALIHQTGGG TGFAFSRLRP
PGAVVKSSKG TASGPVSFMR IFDAATNEIK QGGKRRGANM GILRVDHPDI LEFIHCKEEG
GITNFNISVT ITDAFMEAYE KDTDYDLIDP RDGKAVGKLN ARRVFDEIAE GAWRTGDPGL
VFIDRINKST ANPVPPLGPI ESTNPCGEQP LYPYDSCNLG SIFLTYFVKE GQDDRGLPAV
RQVDWEKLRK VTRLSVRFLD NVIEMNPYPL GAIRKISLAI RRIGLGVGGW ADMLIYLGIP
FDSDEALALG EEIMKVIQEE AIIETRKLAR QRGAFPMFPV SIYKDEKPRR NSTVTTIAPT
GSISIIAGAS SGVEPIFAIA FQHIVKDRHL DRTLTFFNPK FEEIAKSRGF LTEEIKKKVA
EHGVVRDIYE IPEDVRQIFG TAHEIHHDWH IKHQAVFQKY TENAVSKTIN MTNNVTVDDI
KNAYLLAWKT DCKGITVFRD GCKDAQVLNL GVNGKKQGKE VTFEEVWERP MVVSGSTYKI
KTPVGTAFIT VNHDAKGGPI EVFINVGKAG SDVQAMAEAL GRVISKSLKF HSSLTSREKA
EVIIDQLKGI GGRRSVGFGP NKILSLPDAI AMALATNLGL RVNGFLTSPL NGKVAEVFQN
GNSASAHAMS NGSGVQSDLA GAVMSAQYPA QSGTEFSSGD DHTTALAESN LTSVKVGDQL
TLSSTQIPRI AGDICPSCGA SSFVYEEGCA KCFSCGYSEC
//
