ID A0A1J4Z6V7_9BACT Unreviewed; 796 AA.
AC A0A1J4Z6V7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=AUJ89_05010 {ECO:0000313|EMBL:OIO79441.1};
OS Candidatus Omnitrophica bacterium CG1_02_43_210.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805286 {ECO:0000313|EMBL:OIO79441.1, ECO:0000313|Proteomes:UP000182209};
RN [1] {ECO:0000313|EMBL:OIO79441.1, ECO:0000313|Proteomes:UP000182209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_43_210 {ECO:0000313|EMBL:OIO79441.1};
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: 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:OIO79441.1}.
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DR EMBL; MNXF01000046; OIO79441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4Z6V7; -.
DR STRING; 1805286.AUJ89_05010; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000182209; 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 InterPro; IPR024434; TSCPD_dom.
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 Pfam; PF12637; TSCPD; 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 1..82
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 86..401
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 407..554
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 648..715
FT /note="TSCPD"
FT /evidence="ECO:0000259|Pfam:PF12637"
SQ SEQUENCE 796 AA; 88209 MW; 5CFCBC16ED1FC0EF CRC64;
MKLTENAKTV LEKRYLRKDE NGAPVEKPEE MLRRVAANIA QADRFYDRAA DVRKTEDEFY
SLMSELEFLP NSPTLMNAGR DLQQLSACFV LPIEDSMEGI FETLKLTALI HKSGGGTGYS
FSRLRAQGSQ VKSTSGIASG PISFLRVFDA ATQAVKQGGT RRGANMGILR VDHPDILEFI
TCKEDDKSIT NFNISVAVTD EFMEKVESGE EYDLVDPHNN KPLRKLKARD VFELIIKQAH
KNGEPGIIFI DRMNKDNPTP KIAKIESTNP CGEQPLLPYE SCNLGSINLA KMLIETGSKF
EMDWQKLAKV THSAVHFLDN VIDMNKYPVK KIDQMTRSNR KIGLGVMGFA DMLIALGIPY
SSDEAVALAE RVMKFMLDEA TKASVMLAKK RNPFPNYRDS IFAGTTPLRN ATLTTIAPTG
TLSIIASCSS GVEPIFSLCF YRKVLDGAKL MEVNPYFEKV AREKGFYSEG LMKKVSQHSS
IKDISEIPED VRRVFVTAHD ITPLWHIKMQ AAFQKYTNNA VSKTVNFPYQ ASPEDVKEVY
TLAYKLGCKG VTIYRDGSRS EQVLNIDRGS RTTESNLDVT DGTKDAMEKH EKNEELDKVI
NQLQPAKEKI APRPRPKVVC GTTTKIQTGC GNLYVTINED EHNRPFEVFT QMGKAGGCAA
SQLEAVGRLV SLALRSGIDI KSIIDQLEGI RCPSPSWEKG GRIFSCADGL AKVIERILLK
KNKPNTTFAK IEDMTESMGK DKNGRGQDFG DEQYYGKTAT KAKASAVVGV CPDCGGALVY
QEGCMICHSC AYTKCG
//
