ID A0A1J4X596_9BACT Unreviewed; 1106 AA.
AC A0A1J4X596;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=AUJ46_04125 {ECO:0000313|EMBL:OIO53909.1};
OS Candidatus Peregrinibacteria bacterium CG1_02_54_53.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1805323 {ECO:0000313|EMBL:OIO53909.1, ECO:0000313|Proteomes:UP000183121};
RN [1] {ECO:0000313|EMBL:OIO53909.1, ECO:0000313|Proteomes:UP000183121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_54_53 {ECO:0000313|EMBL:OIO53909.1};
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|ARBA:ARBA00025437, 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:OIO53909.1}.
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DR EMBL; MNWP01000024; OIO53909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4X596; -.
DR STRING; 1805323.AUJ46_04125; -.
DR Proteomes; UP000183121; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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 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 37..137
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 188..683
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 740..844
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1106 AA; 122925 MW; BBBD9A735F444F3F CRC64;
MHHEKGLAVR RVFTTPGNDP LEEVTYERRT SRIKNTDGSV VFEMEGAEIP ATWSQMATDI
MVSKYFRRAG IPQVDAQDNL LHDAQDNVVT GSERSVKQVI RRLAGCWRHW GQQEGYFETA
QDAQAFEDEL SYMLVHQMAA PNSPQWFNTG LYYAYGITGP AQGHYYADPK TGEVRESTDS
YTHPQPHACF ILSVNDDMVN PGGIMDLWVR EARLFKYGSG TGSNFSKLRA AGEPLSGGGM
SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VCLDLDHPDI VEFIEWKLKE EKKVAALADA
GYSTDFNDEA YQTVSGQNSN NSVRIPHTFF EAVENDADWD LVWRTEKRRA QEEDRTPAAC
RAIRARELWD KIGFAAWVCA DPGVQYDTTV NDWHTCPAAG RINASNPCSE YMFVDNTACN
LASLNVLKFY DEEHGTFNAE AFQHAVRLWT IVLEISVLMA QFPSREIAEL SYRYRTLGLG
HANLGAMLMR MGIAYDSPEA RAWAGVLTAI MTGESYAASA EMAEKLGTFE GFEENREQML
RVIRNHRRAV YDAPAREYED LHVLPVGIDQ RLAPQDLLVR AKECWDRALA HGERHGYRNA
QVTVIAPTGT IGLLMDCDTT GIEPDFALVK FKKLAGGGYM KIVNQSMQSA LRLLGYSQSQ
MADILQHIQG TLSLEGAPFI NRDSLNRKGF TDEDIAKIEK SLPQVFDFRS VFTKWTLSQE
TLTRLGFSPE RTDDPSFDLL SALGFTEEQI EAANLVVCGQ MTVEGAPHLK PEHLSVFDCA
SRCGKHGKRL ISVEGHIRMM AAVQPFITGA ISKTINLPNE ATVEDIQNAY LLSWKLGLKA
NALYRDGCKL SQPLAARSRK RAKKETESEK APVQREVVEK IVVKEVPRRR KLPDERPSLT
HKFSVAGHEG YLHVGLYEDG KPGEIFIKMA KEGSTLSGVM DTLALSLSMN LQYGVPLEVL
CEKLVRTRFE PMGMSTNKEI PMVQSLMDYL GRWLALKFLP KETALRFHNH DLVEQAYREG
SKSKDAFAMS LPIVDEGATG GYVRVAQTAL PDEDSEQTTA PRISHIETAR QQGFTGSICS
GCGGVRVKRN GSCEVCLDCG ATSGCS
//
