ID A0A0E3ZIM5_9BURK Unreviewed; 988 AA.
AC A0A0E3ZIM5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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=CL55_00002090 {ECO:0000313|EMBL:AKD24542.1};
OS Polynucleobacter duraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=1835254 {ECO:0000313|EMBL:AKD24542.1, ECO:0000313|Proteomes:UP000061135};
RN [1] {ECO:0000313|EMBL:AKD24542.1, ECO:0000313|Proteomes:UP000061135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-MoK4 {ECO:0000313|EMBL:AKD24542.1,
RC ECO:0000313|Proteomes:UP000061135};
RA Hahn M.W.;
RT "Genome of Polynucleobacter strain MWH-MoK4.";
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}.
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DR EMBL; CP007501; AKD24542.1; -; Genomic_DNA.
DR RefSeq; WP_046329494.1; NZ_CP007501.1.
DR AlphaFoldDB; A0A0E3ZIM5; -.
DR STRING; 1835254.CL55_00002090; -.
DR KEGG; pdq:CL55_00002090; -.
DR PATRIC; fig|576611.7.peg.210; -.
DR HOGENOM; CLU_000404_3_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000061135; 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; 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 50..150
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 171..260
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 149..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 988 AA; 109453 MW; D0E4B890E1EAB499 CRC64;
MTYANPQAVG QTIGINNPGI SSSESMNQAP SAGFVAGGVG GGQATQLSDY KIIRRNGSVV
AFEPSKIAIA VTKAFLAVNG GQGAASARVR EQVEQLTHAV VRALLRSRPN GGTFHIEDIQ
DQVELALMRS GEHNVARAYV LYREKRNQER AAQQTNAQET QASTQATEPG LKVSDNGVEK
LLDMAALRTI IEAACEGLGN NIDASPIITE TIKNLYDGVP MAQVYDSAIL ASRTLIEKDP
AYSQVTARIL MHVIRKEILG REVLQGDMQA EYGSYFAKYI NEGISAELLD PRMREFDLPR
LAAALNASRD LQFNYLGLQT LYDRYFLHIE DRRIEMPQAF FMRVAMGLSL NELDRERRAI
EFYEILSTFD FMSSTPTLFN SATTRPQLSS CYLTTVDDDL DGIYEALKEN ALLSKFAGGL
GNDWTNVRAL GSHIKGTNGK SQGVVPFLKV VNDTAVAVNQ GGKRKGAVCA YLETWHLDIE
EFLELRKNTG DDRRRTHDMN TSNWIPDLFM KRVMEGGEWT LFSPSNTPDL HDKFGKAFEE
AYVAYEKKAD AGELKPFRRI PAQQLWRKML GMLFETGHPW ITFKDPCNIR SPQQHIGVVH
SSNLCTEITL NTNESEIAVC NLGSVNLTAH MTTDASGKMI LDHEKLQKTI RTAMRMLDNV
IDINYYAVAK ARNSNLKHRP VGMGIMGFQD CLHMQRIPYA SDEAVKFADS SMEAVCYYAY
QASNELAEER GVYSTYKGSL WDRGILPQDS VALLAAERGG YLEVDSSSTM NWDSLRARIK
EHGMRNSNCV AIAPTATISN IIGVSACIEP TFQNLFVKSN LSGEFTVVNE YLVRDLKDRG
LWDEVMIADL KYFDGTLSKI DRVPQDLRDL YATAFEVEPS WLVEAASRRQ KWIDQAQSLN
IYMGGASGKK LDDTYKLAWL RGLKTTYYLR TMAATHVEKS TVASGQLNAV SSGGGVNGTD
AASAQELDGP ACTMRPGDAG FEECEACQ
//
