ID J3MBN5_ORYBR Unreviewed; 738 AA.
AC J3MBN5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB06G14290.1};
RN [1] {ECO:0000313|EnsemblPlants:OB06G14290.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB06G14290.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB06G14290.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
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|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|RuleBase:RU003410}.
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DR AlphaFoldDB; J3MBN5; -.
DR STRING; 4533.J3MBN5; -.
DR EnsemblPlants; OB06G14290.1; OB06G14290.1; OB06G14290.
DR Gramene; OB06G14290.1; OB06G14290.1; OB06G14290.
DR eggNOG; KOG1112; Eukaryota.
DR HOGENOM; CLU_000404_1_1_1; -.
DR OMA; YIVYRDQ; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006038; Chromosome 6.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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:SF29; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT DOMAIN 524..546
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 738 AA; 83485 MW; B55881B4E0AF7D7B CRC64;
MNCFWFIVLC ERLDSKRCGC RIKDMYGHVN ERSGLNAPLV ADDVYEIIMK NASRLDSEII
YDRDFDYDYF GFKTLERSYL LKLGGRVVER PQHMLMRVSV GIHKDDIESA IKTYHLMSQR
WFTHASPTLF NAGTPRPQLS SCFLICMKDD SIEGIYDTLK ECAVISKSAG GIGVSVHNIR
ATGSYIRGTN GTSNGIVPML RVFNDTARYV DQGGGKRKGA FAVYLEPWHA DVFEFLDLRK
NHGKEEHRAR DLFYALWVPD LFMQRVQNNE EWSLFCPNEA PGLADCWGNE FENLYKKYER
EGKAKKVVPA QTLWFDILKA QIETGTPYML YKDTCNRKSN QQNLGTIKSS NLCTEIIEFT
SPSETAVCNL SSIALPRFVR EKSVPIESHP SKLVGSNGSK NRYFDFDKLA EVTSTVTYNL
NKIIDINYYP VETAKRSNMR HRPIGIGVQG LADTFILLGM PFDSPEAQQL NKDIFETIYY
HALQASAELA AKEGPYETYQ GSPVSKGILQ PDMWNVVPSD RWNWTALRST ISKVGVRNSL
LVAPMPTAST SQILGNNECF EPYTSNIYAL SLIHGEFVVV NKHLLHDLTE MGVWTPALKN
KIIYEDGSVQ KMTEIPDDLK AIYKTVWEIK QKNLVDMAVD RGCYIDQSQS LNVHMEQPNF
GKLTSLHFHA WSKGLKTGMY YLRTRAAADA IKFTVDTSLL KANGENGTKP AEEEDVEAKM
AQVVCSLNNR EECLACGS
//
