UniProt: A0A160N441

Database: UniProt
Entry: A0A160N441_9GAMM

LinkDB:  A0A160N441_9GAMM 
Original site:  A0A160N441_9GAMM

All links

Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (2)   
All databases (19)   

Download RDF

ID   A0A160N441_9GAMM        Unreviewed;       816 AA.
AC   A0A160N441;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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};
GN   ORFNames=ATSB10_32160 {ECO:0000313|EMBL:AND70670.1};
OS   Dyella thiooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=445710 {ECO:0000313|EMBL:AND70670.1, ECO:0000313|Proteomes:UP000077255};
RN   [1] {ECO:0000313|EMBL:AND70670.1, ECO:0000313|Proteomes:UP000077255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATSB10 {ECO:0000313|EMBL:AND70670.1,
RC   ECO:0000313|Proteomes:UP000077255};
RA   Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA   Madhaiyan M.;
RT   "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT   isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
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; CP014841; AND70670.1; -; Genomic_DNA.
DR   RefSeq; WP_063673678.1; NZ_CP014841.1.
DR   AlphaFoldDB; A0A160N441; -.
DR   STRING; 445710.ATSB10_32160; -.
DR   KEGG; dtx:ATSB10_32160; -.
DR   PATRIC; fig|445710.3.peg.3218; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000077255; Chromosome.
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   CDD; cd01679; RNR_I; 1.
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; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077255}.
FT   DOMAIN          36..125
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   816 AA;  90132 MW;  D3EA6A38C5AD9B5C CRC64;
     METLEPAIRE HAVPAPFVRD ASDDFALTPP HNPGQMRVTK RNGGQEIVDV NKIVKAVTRS
     ADGLHGVDPL RVALKTIGGL YDGATTQELD QLSIRTAAAL TAEEPEYGQL AARLLSAFID
     KEVAGQEIQS FSQSIAHGAE VGILNERLRD FVALNARKLN DATDPLASRR FEYFGLRTVY
     DRYLLRHPTK RYVIETPQYF FMRIACALGG NDIAETLELY RLLSALEYIA SSPTLFNAGT
     THEQLSSCFL LDSPVDSLES IYDKYADVAK LSKFAGGIGL AYSRVRSRGS LIKGTNGHSN
     GLVPWLKTLD ASVAAVNQGG KRKGAACVYL EPWHADIEEF LELRDNTGDE ARRTHNLNLA
     NWIPDEFMRR VETDGDWSLF DPKVVPHFVD SWGATFEAAY RSAEAEGLAV KTVKARELYA
     RMLRTLAQTG NGWVTFKDRC NATSNQTAKP DNVIHLSNLC TEILEVTSAG ETAVCNLGSV
     NLARHVVDGA FDFEQLAATV RTAVRQLDRV IDLNFYPIAT ARSANMKWRP VGLGVMGLQD
     VFFKLRLPFD SAEALALSTR IAEEIYFHAL SQSNELAMEH GAHPGFAESR AANGELQFDY
     WPNAQPHELP RWEALRESVK AHGLRNSLLV AIAPTATIAS IAGCYECIEP QVSNLFKRET
     LSGDFLVVNR YLVDELKTLG LWTAEVRDQI KLAEGSIQGI AAIPERLRTI YRTVWELPQK
     ALIELAAARG AYIDQSQSLN LFMENPNIGQ LSSMYMFAWK AGIKTTYYLR SRPATKIAKA
     TVSAGKAVAE PPAEQDQATA AVFCSLENPE YCEACQ
//

DBGET integrated database retrieval system