ID F2L907_BURGS Unreviewed; 993 AA.
AC F2L907;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=bgla_1g05330 {ECO:0000313|EMBL:AEA59226.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA59226.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA59226.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA59226.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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; CP002599; AEA59226.1; -; Genomic_DNA.
DR RefSeq; WP_013696583.1; NC_015381.1.
DR AlphaFoldDB; F2L907; -.
DR STRING; 999541.bgla_1g05330; -.
DR KEGG; bgd:bgla_1g05330; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008316; 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 38..138
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 154..243
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..26
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 993 AA; 108953 MW; 796C93BB43E9492A CRC64;
MQTTDTGTSQ FESAQSRPLG TASQGAPALA PQATFADYKV IRRNGSVVAF EPSKIAIAVT
KAFLAVNGGQ GAASARVREL VEQLTQSVVR ALLRSRPNGG TFHIEDIQDQ VELALMRGGE
HNVARAYVLY REKRHLERAH SDAPVETPDG SSGLTVTDKG VSRPLDMKAL HGLVAAACEG
LGSAVNPDPI VAETVKNLYD GVPLSQVYDS AILAARTMIE KDPAYSQVTA RILLHTIRRE
ILGEEVAQGE MQARYAEYFP QFLKRGVEAE LLDDKLLQFD LVRLGEALDA SRDLQFGYLG
LQTLYDRYFL HVEGTRIEMP QAFYMRVAMG LALNEIDREA RAIEFYNVLS SFDFMSSTPT
LFNSGTRRSQ LSSCYLTTVA DDLDGIYEAL KENALLSKFA GGLGNDWTRV RALGSHIKGT
NGKSQGVVPF LKVVNDTAVA VNQGGKRKGA VCAYLESWHL DIEEFLELRK NTGDDRRRTH
DMNTANWIPD LFMKRVMEGG DWTLFSPSTC PDLHDKFGAE FEAAYLGYEE KVARGELKLF
KKIPAAQLWR KMLGMLFETG HPWITFKDPC NIRSPQQHVG VVHSSNLCTE ITLNTSDSEI
AVCNLGSVNL VAHLAKQADG SYALDHDKLK RTVSVAMRML DNVIDINYYA VAKARNSNLK
HRPVGLGIMG FQDCLHLLRT PFSSDTAVEF ADRSMEAVCY YAYWASTELA EERGRYSSYT
GSLWDRGILP QDTLKLLEEA RGGYVEVDMS ESLDWTSLRG RISVHGMRNS NCIAIAPTAT
ISNIIGVSPC IEPTFQNLFV KSNLSGEFTV VNEYLVRDLK ERGLWDEVMV ADLKYFDGML
SRIDRIPADL RAIYATAFEV DPKWLVEAAS RRQKWIDQAQ SLNIFMAGAS GKKLDEIYKL
AWVRGLKTTY YLRTMAATHV EKSTVAHGAL NAVPSSGGMG GGSAGGAQGA GSFGAAGGAA
PTGALSAAPI EADGPVCTMR PGDPGFEECE ACQ
//
