ID A0A368L2J2_9BURK Unreviewed; 947 AA.
AC A0A368L2J2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DU000_08295 {ECO:0000313|EMBL:RCS57600.1};
OS Parvibium lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Parvibium.
OX NCBI_TaxID=1888893 {ECO:0000313|EMBL:RCS57600.1, ECO:0000313|Proteomes:UP000252357};
RN [1] {ECO:0000313|EMBL:RCS57600.1, ECO:0000313|Proteomes:UP000252357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMB9 {ECO:0000313|EMBL:RCS57600.1,
RC ECO:0000313|Proteomes:UP000252357};
RX PubMed=29498621; DOI=10.1099/ijsem.0.002667;
RA Chen W.M., Xie P.B., Hsu M.Y., Sheu S.Y.;
RT "Parvibium lacunae gen. nov., sp. nov., a new member of the family
RT Alcaligenaceae isolated from a freshwater pond.";
RL Int. J. Syst. Evol. Microbiol. 68:1291-1299(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCS57600.1}.
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DR EMBL; QPGB01000003; RCS57600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368L2J2; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000252357; Unassembled WGS sequence.
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:UP000252357}.
FT DOMAIN 11..111
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 129..218
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 947 AA; 105761 MW; 2FAEBEE8A643BEB7 CRC64;
MAATATTYSQ YKLIRRNGAV VGFEPSKIAI ALTKAFLAVN GGQGAASARV RELVEGLTQA
VVNALVRRQP AGGTFHIEDV QDQVELSLMR SGEHDVARAY VLYREKRAQE RAKQRETQTA
QSASAEVALQ VVDGGVSRPL DVLAIQSLLQ AACAGLEEHV DPVAIFKETL KNLYDGIPLD
EVYKSAILAA RAMIEKDPAY SQVTARILQH TIRREVLGEE VAPADMAARY ADYFPKFIKR
GIEAQLLDPK LAQFDLKKLA NALLAERDNQ FSYLGLQTLY DRYFLHVEGE RIELPQAFFM
RVAMGLAISE IDRETRAIEF YQLLSSFDFM SSTPTLFNSG TLRPQLSSCY LTTVADDLDG
IYEAIKENAL LAKYAGGLGN DWTPVRAMGS WIKGTNGKSQ GVVPFLKVVN DTAVAVNQGG
KRKGAVCTYL ESWHLDIEEF LELRKNTGDD RRRTHDMNTA NWIPDLFMKR VMENGEWTLF
SPADVPDLHD LYGQAFERAY LRYEEKAAQG ELKLFKKVQA VTLWRKMLGM LFETGHPWIT
FKDPCNIRSP QQHVGVVHSS NLCTEITLNT NDSEIAVCNL GSVNLAAHLT LNAAGSYELN
HEKLQRTVRT AMRMLDNVID INYYSVGKAR NSNLKHRPVG MGIMAFQDCL HMLRIPYASQ
AAVEFADRST EAVCYYAYWA STELAAERGR YSSYPGSLWD RGILPQDSLK LLAQERGGYV
EVDVSETMDW AALRARIQQY GMRNSNCVAI APTATISNII NVSACIEPTY QNLYVKSNLS
GEFTVVNDYL VRDLKRLGLW DEVMIADLKY FDGSLSRIDR IPQDLRDVYA TAFEMDPAWL
VEAASRRQKW IDQAQSLNIY ISAPSGKKLD ETYKLAWLRG LKTTYYLRTM GATHAEKSTS
NRIGQLNSVP SDGGVATSHA LPEPEIVGNV CTLRPGDPGF EECEACQ
//
