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Database: UniProt
Entry: Q1IDP3_PSEE4
LinkDB: Q1IDP3_PSEE4
Original site: Q1IDP3_PSEE4 
ID   Q1IDP3_PSEE4            Unreviewed;       958 AA.
AC   Q1IDP3;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
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:CAK14216.1};
GN   OrderedLocusNames=PSEEN1337 {ECO:0000313|EMBL:CAK14216.1};
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK14216.1, ECO:0000313|Proteomes:UP000000658};
RN   [1] {ECO:0000313|EMBL:CAK14216.1, ECO:0000313|Proteomes:UP000000658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48 {ECO:0000313|EMBL:CAK14216.1,
RC   ECO:0000313|Proteomes:UP000000658};
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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}.
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DR   EMBL; CT573326; CAK14216.1; -; Genomic_DNA.
DR   RefSeq; WP_011532632.1; NC_008027.1.
DR   AlphaFoldDB; Q1IDP3; -.
DR   STRING; 384676.PSEEN1337; -.
DR   GeneID; 32804603; -.
DR   KEGG; pen:PSEEN1337; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_3_0_6; -.
DR   OMA; RGSIQNI; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000000658; 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   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; 2.
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}.
FT   DOMAIN          31..131
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   DOMAIN          147..236
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   958 AA;  106942 MW;  49F01A6782339969 CRC64;
     MQTDTTRENP QALAPQAESN QDLTATAPGQ LRVIKRNGTV VPYTDDKITV AITKAFLAVE
     GGTAAASSRI HDTVARLTEQ VTATFKRRMP SGGTIHIEEI QDQVELALMR AGEQKVARDY
     VIYRDQRAKE RATRANTDAV VEPHPSIRIT LADGSLAPLD MARLNTIISE ACEGLAEVDG
     ELIQRETLKN LYDGVALKDV NTALVMTART LVEREPNYSF VTARLLMDTL RAEGLGFLNV
     ADSATHHEMA DLYAKALPAY VEKGVEFELL DPALKGYDLE RMGKAINHER DQQFTYLGLQ
     TLYDRYFIHK DGVRFELPQV FFMRVAMGLA LEEKDKEARA IEFYNLLSSF DYMASTPTLF
     NAGTLRPQLS SCYLTTVPDD LSGIYHAIHD NAMLSKFAGG LGNDWTPVRA LGSYIKGTNG
     KSQGVVPFLK VVNDTAVAVN QGGKRKGAVC AYLETWHLDI EEFIELRKNT GDDRRRTHDM
     NTANWIPDLF MKRVFDDGKW TLFSPSEVPD LHDLTGKAFE ERYEYYEALT EYNKIKVFKT
     IQAKDLWRKM LSMLFETGHP WLTFKDPCNL RSPQQHVGVV HSSNLCTEIT LNTNKDEIAV
     CNLGSINLPN HIVDGKLDTA KLQRTVNTAV RMLDNVIDIN YYSVPQARNS NFKHRPVGLG
     IMGFQDALYL QHIPYGSDAA VEFADKSMEA VSYYAIQASC DLADERGAYE TFQGSLWSKG
     ILPLDSQQIL IEARGQKYID VDLTESLDWA PVRERVKKGI RNSNIMAIAP TATIANITGV
     SQSIEPTYQN LYVKSNLSGE FTVINPYLVR DLKARGLWDS VMINDLKYYD GSVQQIERIP
     QELKDLYATA FEVETKWIVD AASRRQKWID QAQSLNLYIA GASGKKLDVT YRMAWYRGLK
     TTYYLRALAA TSTEKSTINT GKLNAVSSGG DSAPVQAAGP APVPKACAID EPDCEACQ
//
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