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
//