ID A0A0S8BRB2_9PROT Unreviewed; 658 AA.
AC A0A0S8BRB2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE Flags: Fragment;
GN ORFNames=AMJ67_16525 {ECO:0000313|EMBL:KPK14178.1};
OS Betaproteobacteria bacterium SG8_41.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK14178.1, ECO:0000313|Proteomes:UP000051544};
RN [1] {ECO:0000313|EMBL:KPK14178.1, ECO:0000313|Proteomes:UP000051544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_41 {ECO:0000313|EMBL:KPK14178.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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:KPK14178.1}.
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; LJTT01000109; KPK14178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BRB2; -.
DR STRING; 1703391.AMJ67_16525; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000051544; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 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; 2.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 32..132
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 146..237
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT NON_TER 658
FT /evidence="ECO:0000313|EMBL:KPK14178.1"
SQ SEQUENCE 658 AA; 73628 MW; E18380F95B147E8F CRC64;
MQVATETLRV ATDANLPPAE LPAGNEERYA QYKVIRRNGA VVGFEPSKIV IAMTKAFIAV
NGGTGAASAR VREQVTKLTE SVVSALMRRH PSGGTLHIED IQDQVELALM REGEHNVARA
YVLYREERAR ERAKERHLQD EIRGNTTITV KDGGVAKPLD LAAIAALVRD ACEGLGRDVG
PGPILQAMQR DLYDGVPMAE VRKSLVLAAR GLIEQDPGYS YVTARLLLHT LRLETLGEEV
TQAEMHLRYA EYLPRFVETG IEAGLLDERL ANFDLKCLGA ALDANRDLKF TYLGLQILYD
RYFLHVQGSR IELPQIFFMR VAMGLALNET EDQREARAIE FYNVLSSFDF MSSTPTLFNS
GTRRSQLASC YLTTVSDDLD GIYEAIKENA LLQKFAGGLG NDWTPVRALG AHIKGTNGKS
QGVVPFLKVV NDTAVAVNQG GKRKGAVCSY LETWHLDIEE FLELRKNTGD DRRRTHDMNT
ANWVPDLFMK RVMENGDWTL FSPSDVPDLH EKYGKAFERA YLEYERRAAT GELKLYKKVP
ATQLWRKMLS MLFETGHPWI TFKDPCNIRS PQQHVGVVHS SNLCTEITLN TGADEIAVCN
LGSVNMPAHL DTSTGRIDME KLRRTVSTAM RMLDNVIDLN FYSVNKARNS NFKHRPVG
//
