ID E6WP17_PSEUU Unreviewed; 814 AA.
AC E6WP17;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=Psesu_0053 {ECO:0000313|EMBL:ADV25916.1};
OS Pseudoxanthomonas suwonensis (strain 11-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV25916.1, ECO:0000313|Proteomes:UP000008632};
RN [1] {ECO:0000313|EMBL:ADV25916.1, ECO:0000313|Proteomes:UP000008632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA Hugenholtz P., Gladden J., Woyke T.;
RT "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL Submitted (JAN-2011) 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; CP002446; ADV25916.1; -; Genomic_DNA.
DR RefSeq; WP_013533746.1; NC_014924.1.
DR AlphaFoldDB; E6WP17; -.
DR STRING; 743721.Psesu_0053; -.
DR KEGG; psu:Psesu_0053; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008632; 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; 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:UP000008632}.
FT DOMAIN 52..145
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 91546 MW; 63D275055D7D803E CRC64;
MTSQDTSSPV ATPADPVVAA ARAARAIDPN DHVPLPPAAS GSAHPPEAEA TTWITKEAGN
RRLAFDPARL ERSIDVIAAG FPQLEIGDYK RAVLGFVARK PALSADDLVD HLIREAEARV
DLTAPEWERF AARLYLRRLY KRASRNRFYD AGQKYGSYVG LQESLADRGI YSNDILRAYS
KEELEEAGRM IEPERDKLFA YNGLYLLATR YLATDTARNV YELPQERWLT IALYLMQEEK
PRERRMQLVG EAYWALSNLY MTVATPTLQN AGKVGGQLSS CFIDTVDDSL QGIYDSNTDI
ARVSKGGGGV GAYLGYVRAA GAPIRGVPNS SGGVVPWIKQ LNNTAVSVDQ LGQRKGAVAV
YLDIWHRDIE AFLDLRLNNG DQRLRAHDVF TAVCIPDLFM EAVERRGDWY LFDPHEVKQA
KGWYLQDFYD ERRGEGSFRS KYQELVEDGR IGRRTVKAID LFKRIMVSQL ETGNPFMFYR
DEVNRKNPNK HCGTVYSSNL CTEILQNQSP TRMIQEVISG NQIVTTRQAG DFVVCNLSSI
NLGRAVVQAD GQGDLISDVL ERLVPIQVRM LDNVIDLNQL PVPQATITNR RYRAIGLGTF
GWHHLLALKG IHWDSKEAED YSDALYERIN RLAIQASMEL AKEKGTYPAF PGSDWHTGAY
FRERGYNSPE WLDLAAQVAV NGLRNGWLLA VAPNMSTAQI AGSSASIDPV YSAFYYEEKK
DYRRPVAAPG LSLETWPYYE KGAWKVDQFA SVRQNARRQR HVDQAISFNL YVPSSIRASV
LLELHLEGWR QGLKTTYYVR SNDIDVAECE WCSS
//
