ID A0A212DWV8_9BACT Unreviewed; 753 AA.
AC A0A212DWV8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=US76_01755 {ECO:0000313|EMBL:OWK26811.1};
OS Parcubacteria group bacterium GW2011_GWA2_38_13b.
OC Bacteria.
OX NCBI_TaxID=1618780 {ECO:0000313|EMBL:OWK26811.1, ECO:0000313|Proteomes:UP000034916};
RN [1] {ECO:0000313|EMBL:OWK26811.1, ECO:0000313|Proteomes:UP000034916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW2011_GWA2_38_13b {ECO:0000313|EMBL:OWK26811.1};
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).
RN [2] {ECO:0000313|EMBL:OWK26811.1, ECO:0000313|Proteomes:UP000034916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW2011_GWA2_38_13b {ECO:0000313|EMBL:OWK26811.1};
RX PubMed=28067254; DOI=10.1038/srep40101;
RA Castelle C.J., Brown C.T., Thomas B.C., Williams K.H., Banfield J.F.;
RT "Unusual respiratory capacity and nitrogen metabolism in a Parcubacterium
RT (OD1) of the Candidate Phyla Radiation.";
RL Sci. Rep. 7:40101-40101(2017).
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:OWK26811.1}.
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DR EMBL; LBUF02000018; OWK26811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212DWV8; -.
DR STRING; 1618780.US76_C0011G0040; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034916; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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; PF03477; ATP-cone; 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.
DR PROSITE; PS51161; ATP_CONE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 6..99
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 694..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83818 MW; 40EFC772C2B99D13 CRC64;
MVNKIIKIKK RDGRIVPFNK SKITNAIYKA VRVVGRKNGK LSRRLCDQAV AVLNERFTEK
DIPMVEEIQD IVEEVLIKAG ESQTAKAYIL YRQKRKEIRE AKYFLLAQDI KTTLSENALK
VLEARYLRKD ANGKVQETPQ KMFQRVASNI AAAEKIYNPK ISDDALFMIE EKFYRMMASL
EFLPNSPTLM NAGGALQQLS ACFVLPVEDD MASIFEAVKN TALIHQTGGG TGFNFSRLRP
KGSPVKSTQG IASGPISFMT VFDAATNVVK QGGKRRGANM GILRIDHPDI LDFIVCKDKE
GMLPNFNISV AVSDKFMEAL ENNGKYDLIN PKNNQSVGKL DATEVFDLIT KHAWNNGEPG
IIFIDNINRD NPTPKFGPIE STNPCAEQPL LPFESCNLGS INLTKVIIKK ANSRKINWNK
LKRIIHDAVH FLDNVIDMNH YPLPAIEIMT KGNRKIGLGL MGFADMLIKL SIPYDSDRAL
RIAEEIMGFI QKEAKEASAA IAVKRGLFPN FRDSVYDVSG TMNTVKVRNA TVTTIAPTGT
IAVIAGCSSG IEPHFALAYT RISYIAQNDN NGADKGVELV EVNPLFEEIA KKRGFYDSNL
MKEVAEKGSV QDIKGIPVDV KRIFVTSLDI APEWHIKIQA AFQKYVDNAV SKTINFPFSA
AVEDVKKSYL LAYKSGCKGV TIYRNESRKQ QVLNIGKKYK EGENKNPEKP DSKKPVNEAS
QEIIPEKIID PELKNPEPYM PDLPPGSCPT CTI
//
