ID B4E5V9_BURCJ Unreviewed; 1003 AA.
AC B4E5V9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=BCAL3429 {ECO:0000313|EMBL:CAR53752.1};
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591 {ECO:0000313|EMBL:CAR53752.1, ECO:0000313|Proteomes:UP000001035};
RN [1] {ECO:0000313|EMBL:CAR53752.1, ECO:0000313|Proteomes:UP000001035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
RC CF5610 {ECO:0000313|Proteomes:UP000001035};
RX PubMed=18931103; DOI=10.1128/JB.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR53752.1; -; Genomic_DNA.
DR AlphaFoldDB; B4E5V9; -.
DR KEGG; bcj:BCAL3429; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001035; 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}.
FT DOMAIN 40..140
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 158..247
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 110045 MW; BA56FA2E3F7B623D CRC64;
MHMQTTDNAT SQYESASSRP LGGTEQGAKA LAPQATFADY KVIRRNGSVV SFEPSKIAIA
VTKAFLAVNG GQGAASARVR EQVEQLTHNV VRALVRSRPN GGTFHIEDIQ DQVELALMRG
GEHNVARAYV LYREKRHLER QHAGEEAAAA GGESTTGINV VDNGVTRPLD LNALRALIVS
ACDGLGAAVN PDPIVAETVK NLYDGVPMSQ VYDSAILAAR TMIEKDPAYS QVTARILLHT
IRREILGEEV VQAEMSTRYA EYFPQFLKRG VDAGLLDDKL LQFDLKRLGE ALDANRDLQF
GYLGLQTLYD RYFLHVDGTR IEMPQAFFMR VAMGLSLNEI DRETRAIEFY NVLSSFDFMS
STPTLFNSGT HRSQLSSCYL TTVADDLDGI YEALKENALL SKFAGGLGND WTRVRALGSH
IKGTNGKSQG VVPFLKVVND TAVAVNQGGK RKGAVCAYLE SWHLDIEEFL ELRKNTGDDR
RRTHDMNTAN WIPDLFMKRV MEGADWTLFS PSTCPDLHDK FGADFEKAYT AYEDKVARGE
IKLFKKIPAQ QLWRKMLGML FETGHPWITF KDPCNVRSPQ QHVGVVHSSN LCTEITLNTS
DTEIAVCNLG SVNLVAHLVK QADGSYALDH DKLKRTISVA MRMLDNVIDI NYYAVPKARN
SNLKHRPVGM GIMGFQDCLH LLRTPYASEA AVEFADRSME AVCYYAYYAS TELAEERGRY
SSYRGSLWDR GILPQDTLKL LTEARGGYVE VDTSESLDWT TLRSRIAAHG MRNSNCVAIA
PTATISNIIG VSACIEPTFQ NLYVKSNLSG EFTVVNEYLV RDLKERGLWD EVMVADLKYF
DGMLSRIDRI PADLRAIYAT AFEVDPTWLV EAASRRQKWI DQAQSLNIYM GGASGKKLDE
VYKLAWLRGL KTTYYLRTMA ATHVEKSTVA HGALNAVPTG GAGSGGSGSG GAQGAAGGFG
AAGGDASSGA INAAPALAPV EADGPVCTMR PGDPGFDECE ACQ
//
