GenomeNet

Database: UniProt
Entry: D8MUR7_ERWBE
LinkDB: D8MUR7_ERWBE
Original site: D8MUR7_ERWBE 
ID   D8MUR7_ERWBE            Unreviewed;       761 AA.
AC   D8MUR7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 66.
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   Name=nrdA {ECO:0000313|EMBL:CAX60574.1};
GN   OrderedLocusNames=EbC_30430 {ECO:0000313|EMBL:CAX60574.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX60574.1, ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX60574.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX60574.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
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   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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; FP236843; CAX60574.1; -; Genomic_DNA.
DR   RefSeq; WP_013203059.1; NC_014306.1.
DR   AlphaFoldDB; D8MUR7; -.
DR   STRING; 634500.EbC_30430; -.
DR   KEGG; ebi:EbC_30430; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_3_0_6; -.
DR   OMA; RGSIQNI; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000008793; 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:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1650.20; -; 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:UP000008793}.
FT   DOMAIN          5..95
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   761 AA;  85786 MW;  B2BAA55CA040E164 CRC64;
     MNQSLLVTKR DGRTERINLD KIHRVLDWAA EGLQNVSVSQ VELRSHIQFY EGIRTSDIHE
     TVIKSAADLI SRDAPDYQYM AARLAIFHLR KKAYGQFEPP KLYDQVKRMV DMGKYDRHLL
     EDYSAEEFEQ MDGFIDHWRD MNFSYAAVKQ LEGKYLVQNR VSGDIYESAQ FLYILVAACL
     FSGYPRDTRL DYVKRFYDAI STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT
     SSAIVKYVSQ RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG
     AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG GDITLFSPSD
     VPGLYDAFFA DQDEFERLYT KYENEPSIRK QRVKAVDLFS LMMQERASTG RIYIQNVDHC
     NTHSPFDPAI APVRQSNLCL EIALPTKPLL DVNDENGEIA LCTLSAFNLG AINSLDDLEE
     LATLAVRALD ALLDYQDYPI PAAQRGAMGR RTLGIGVINY AYYLAKHGVR YSDGSANDLT
     HRTFEAIQFY LLKASNELAK EQGACPWFNE TTYAQGIMPI DTYKKDLDAI SSEPLHLDWD
     GLREQIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG HISIKASKDG ILRQVVPEYE
     RLKDSYELLW DMPNNDGYLQ LVGLMQKFID QAISSNTNYD PTRFANGRVP MKQLLKDLLT
     AYKFGVKTLY YQNTRDGAED TQEDLVPSIQ DDGCESGACK I
//
DBGET integrated database retrieval system