ID B2JH27_PARP8 Unreviewed; 997 AA.
AC B2JH27;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=Bphy_2639 {ECO:0000313|EMBL:ACC71811.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC71811.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC71811.1; -; Genomic_DNA.
DR RefSeq; WP_012402013.1; NZ_CADFGH010000021.1.
DR AlphaFoldDB; B2JH27; -.
DR STRING; 391038.Bphy_2639; -.
DR KEGG; bph:Bphy_2639; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001192; Chromosome 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT DOMAIN 39..139
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 151..240
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 109576 MW; F58CEDA9A1BCB810 CRC64;
MQTTDNVTTR FEGAPTGRPV EGLAQGADAL APQTGYADYK VIRRNGSVVS FEPSKIAIAV
TKAFLAVNGG QGAASARVRE LVEQLTQNVV RALVRSRPNG GTFHIEDIQD QVELALMRTG
EHNVARAYVL YREKRTQERG HEVDAPVASG LNVTDNGVTR PLDMAALRGL IESACANLGD
AVNAEPIVAE TVKNLYDGVP MSQVYDSAIL AARTMIEKDP AYSQVTSRIL LHTIRREILE
EEVTQAEMAG RYAEYFPLFI KRGVNAELLD DKLLQFDLKR LGAALDANRD LQFGYLGLQT
LYDRYFLHID GTRIEMPQAF FMRVAMGLSL NEIDREARAI EFYNVLSSFD FMSSTPTLFN
SGTRRSQLSS CYLTTVDDDL DGIYEALKEN ALLSKFAGGL GNDWTRVRAL GSHIKGTNGK
SQGVVPFLKV VNDTAVAVNQ GGKRKGAVCA YLESWHLDIE EFLELRKNTG DDRRRTHDMN
TANWIPDLFM KRVLEGGDWT LFSPSTCPDL HDKFGAEFEA AYTAYEDKVA RGEIKLFKKI
PAAQLWRKML GMLFETGHPW ITFKDPCNVR SPQQHVGVVH SSNLCTEITL NTSDTEIAVC
NLGSVNLVAH LKEQADGTLA LDHDKLKRTI SVAMRMLDNV IDINYYAVAK ARNSNLKHRP
VGMGIMGFQD CLHVLRTPYA SQEAVEFADR SMEAVCYYAY WASTELAEER GRYSTYRGSL
WDRGILPQDT LKLLADARGG YVEVDSSESM DWASLRSRIA THGMRNSNCV AIAPTATISN
IIGVSACIEP TFQNLYVKSN LSGEFTVVNE YLVRDLKARG LWDEVMVADL KYFDGSLSRI
DRVPADLRAI YATAFEVDAT WLVEAASRRQ KWIDQAQSLN IYMAGASGKK LDEVYKLAWL
RGLKTTYYLR TMAATHVEKS TVAHGALNAV PSGDGGAGSF GVGGGAASSG TKGGFQASAA
SAAATSVPAV EAAPEADGPV CMMRPGDPGF EECEACQ
//
