ID A0A1F8T3L0_9CHLR Unreviewed; 856 AA.
AC A0A1F8T3L0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=A2Z45_01430 {ECO:0000313|EMBL:OGO66720.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_55_16.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797669 {ECO:0000313|EMBL:OGO66720.1, ECO:0000313|Proteomes:UP000177674};
RN [1] {ECO:0000313|EMBL:OGO66720.1, ECO:0000313|Proteomes:UP000177674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGO66720.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGOK01000001; OGO66720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8T3L0; -.
DR STRING; 1797669.A2Z45_01430; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000177674; 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; 1.
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 14..93
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 96..640
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 856 AA; 93617 MW; D4737C30868D0145 CRC64;
MPTPPLPADV PQVELTENAR QVFTRRYIRK GGDGSPLESV EETFWRVAYH VAKSEETWGG
DVLQTARQFY ELLSQRRFFP NSPTFTGAGT PLGQLAACFV LPISDDMGRD PAGIFQTLRD
AALIQQTGGG NGFAFSPLRP KGTLVKSSAG QATGPVGFLR VYDRAFGEIA QGGTRRGANM
GVLRVDHPDI EEFITCKTDE NAITNFNISV GITDAFMEAV RNDTYWDLRF PDVSSSEYKG
FRGTLEEAER AGIPITVYKR IGARDLFEKI VLQAHYNGEP GVLFLDAANR SNPVPNLYQL
EATNPCGEQW LGPYENCCLG SVNLAPHFGL DGTVDWEGLR QSVVLSTRFL DDVVQANAYV
PAVPQLKKAA FQARRIGLGI MGLADLMYHV GVRYGSEAGL EFAAQVMEFV RYHAMLTSVD
LAKERGPFEA IKGSIYDPQG LRWQPPEPLT PYVHDWGRPT VEWKDVIDGI RHYGIRNAAQ
TTIAPTGTIA TVAGCEGYGC EPVFALAYIR HVNDNGKDLQ LTYTSPLFEK ALLEAGLDEQ
SQQMIINHIM ETGTCQDLPD LMVEAAGSNG LGLPDTIRET FVVSQDISAE EHVRMQAAMQ
AFVDNSLSKT INFPESATVE DVATAYQLAW ELGCKGITVY VTGSRQKVVL ETHATAKEKR
PFSEMEALDV KAEQLAMWGE TKKPRPRRLP GYTISVNTPL GKTFVTVNEN GGGQPFEVFV
NTAKAGSETA AVSEAIGRLI SYTLRLASSL APRERLIEVW RQLSGIGGGR SLGFGPNRVR
SLPDGVAQAL EEYLQNSAAH ASYQEEEHGN GSHSAVDLLP EQPPLQIGDL CPECGEAALV
NEEGCRKCYA CGYSEC
//
