UniProt: A0A087CK20

Database: UniProt
Entry: A0A087CK20_9BIFI

LinkDB:  A0A087CK20_9BIFI 
Original site:  A0A087CK20_9BIFI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (1)   
All databases (18)   

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ID   A0A087CK20_9BIFI        Unreviewed;       730 AA.
AC   A0A087CK20;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=BREU_2032 {ECO:0000313|EMBL:KFI83620.1};
OS   Bifidobacterium reuteri DSM 23975.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437610 {ECO:0000313|EMBL:KFI83620.1, ECO:0000313|Proteomes:UP000028984};
RN   [1] {ECO:0000313|EMBL:KFI83620.1, ECO:0000313|Proteomes:UP000028984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23975 {ECO:0000313|EMBL:KFI83620.1,
RC   ECO:0000313|Proteomes:UP000028984};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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   -!- 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:KFI83620.1}.
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DR   EMBL; JGZK01000021; KFI83620.1; -; Genomic_DNA.
DR   RefSeq; WP_044090305.1; NZ_JGZK01000021.1.
DR   AlphaFoldDB; A0A087CK20; -.
DR   STRING; 1437610.BREU_2032; -.
DR   eggNOG; COG0209; Bacteria.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000028984; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.1650.20; -; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR026459; RNR_1b_NrdE.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013554; RNR_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028984}.
FT   DOMAIN          582..604
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   730 AA;  81479 MW;  41A925CB8730C6D1 CRC64;
     MTDFTNTELA LDNTSHAAEP TDPAHDYHAL NAMLNLYDSN GKIQFDKDKA AERAYVTNHV
     AANTVTFPST AERLKYLIDN QYYNPAVFAQ YTAGFLDRFY DHVESVGFEF GTFLGAFKFY
     TSYALKTFDG KRYLEDFPQR CAAVALELAA GDEQQAIEYA DEMLAGRFQP ATPTFLNLGK
     AQRGEPVSCF LVRIEDNMES ISRGINAALQ LSKRGGGVAL LLSNLRELGA PIKHIENQSS
     GVIPVMKLLE DSFSYANQLG ARQGAGAVYL SAHHPDILRF LDTKRENADE KIRIKSLALG
     VVIPDITFEL AKQKAQMALF SPYDVERVYG KPFADIAISE HYDEMVADDR IRKTYIDARK
     FFTTIAELQF ESGYPYIVFE DTVNRANPIE GRVTMSNLCS EILQVQEPSE YNEDLTYKHV
     GRDISCNLGS LNIAKAMDGG LAHTVETAIR ALTSVAEHTS INAVPSIRRA NEEGHAIGLG
     QMNLHGFLAR EGIMYGSEEG LDFTDMYFMT VAYHAYRASH ALAVEHGRAF QSFPTSDYAK
     PAGQGNYFDK YTDGRRSLEP RTARVRELFA QFGIAIPTVA DWQALQAAII KDGIYNQNLQ
     AVPPTGSISY INHSTSSIHP IASKIEIRKE GKIGRVYYPA AYMTNDNLKY YKDAYEIGWK
     AIVDTYAEAT QHVDQGLSLT LFFPDTATTR DLNKAQIYAW RKGIKTLYYI RIRQQALEGT
     EVAGCVSCML
//

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