ID A0A176YDG6_9BRAD Unreviewed; 933 AA.
AC A0A176YDG6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AYJ54_24520 {ECO:0000313|EMBL:OAF04022.1};
OS Bradyrhizobium centrolobii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAF04022.1, ECO:0000313|Proteomes:UP000076959};
RN [1] {ECO:0000313|EMBL:OAF04022.1, ECO:0000313|Proteomes:UP000076959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10245 {ECO:0000313|EMBL:OAF04022.1,
RC ECO:0000313|Proteomes:UP000076959};
RA Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (MAR-2016) 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}.
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:OAF04022.1}.
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DR EMBL; LUUB01000088; OAF04022.1; -; Genomic_DNA.
DR RefSeq; WP_063705366.1; NZ_LUUB01000088.1.
DR AlphaFoldDB; A0A176YDG6; -.
DR STRING; 1505087.AYJ54_24520; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000076959; 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}.
FT DOMAIN 32..132
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 149..238
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 933 AA; 103075 MW; ED93216A59D87DC5 CRC64;
MSLNLHDAEI ASAPIIQLRP DSLAATPSEP AMQIIRRNGK VTPFDSSKIA VAMTKAFLAV
EGNTGAASRR VHESVEQLTA DVVAALTRRA GEGRTFHIED VQDQVELALM RSENHKVARA
YVLYREERAR KRAEAEAAAP KAISSQPSLH MLRDDGSNVP VDMARLTAVI AEACNGLDAT
DPAAVLVETT RNLYDGISRN ELALAPIMAA RSLVEQEPNH AYVSARLLLD KLRGEVLTYV
HRQPMDASQA DMGSRYAGYF PVYIKTGIAA ELLDPELTRF DLNRISAALK PERDLQFQFL
GLQTLYDRYL LHVSGNRIEL PQAFFMRVAM GLALREIDRE TKAIEFYDLL SSFDFMASTP
TLFNSGTPRP QLSSCFLTTV TDELDGIFKS IKDNALLAKY SGGLGNDWTP VRGLGAHIKG
TNGESQGVVP FLKVANDTAI AVNQGGKRKG AVCAYLETWH LDIEEFLDLR KNTGDDRRRT
HDMNTANWVP DLFMQRVEAD GEWTLFSPDE APDLHDLYGE AFKTIYEDYE AKAKAGKMRI
FKTVRASDLW RRMLTMLFET GHPWITFKDP CNLRSPQRHA GVIHSSNLCT EITLNTAADE
VAVCNLGSIN LLAHVGREGI DHAKLQRTVK TAMRMLDNVI DVNFYTIPEA RRSNMRHRPV
GLGLMGFQEA LHVQGIAIAS EAAVTFADVS MEAISFHAIE ASSDLASERG PYASFEGSLW
SKGILPIDSI QLLADARGGL DLDRSSRLDW NGLRQKVVAR GMRNSNVMAI APTATISNIC
GVSQSIEPSY QNLFVKSNMS GDFTVVNEFL VRDLKTRGLW DEVMVSDLKY FDGSLDQINR
ALNLYIASPS GKKLDALYRL AWRRGLKTTY YLRSRSATHV EKSTLKGTDG KLNAVSAAAV
VAHAPIDIPS ATAPEFDGIK ACRIEDPECE ACQ
//
