ID Q8GZU9_SOYBN Unreviewed; 809 AA.
AC Q8GZU9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 141.
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 Name=548020 {ECO:0000313|EnsemblPlants:KRH59506};
GN ORFNames=GLYMA_05G186900 {ECO:0000313|EMBL:KRH59506.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:AAN87547.1};
RN [1] {ECO:0000313|EMBL:KRH59506.1, ECO:0000313|EnsemblPlants:KRH59506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH59506};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH59506.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EMBL:AAN87547.1}
RP NUCLEOTIDE SEQUENCE.
RA Xiong X., Cowles J.R.;
RT "Soybean Ribonucleotide Reductase Large Subunit A.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KRH59506}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH59506};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH59506.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH59506.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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|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; AF118784; AAN87547.1; -; mRNA.
DR EMBL; CM000838; KRH59506.1; -; Genomic_DNA.
DR RefSeq; NP_001237526.1; NM_001250597.1.
DR AlphaFoldDB; Q8GZU9; -.
DR SMR; Q8GZU9; -.
DR STRING; 3847.Q8GZU9; -.
DR PaxDb; 3847-GLYMA05G32070-1; -.
DR EnsemblPlants; KRH59506; KRH59506; GLYMA_05G186900.
DR GeneID; 548020; -.
DR Gramene; KRH59506; KRH59506; GLYMA_05G186900.
DR KEGG; gmx:548020; -.
DR eggNOG; KOG1112; Eukaryota.
DR HOGENOM; CLU_000404_1_0_1; -.
DR InParanoid; Q8GZU9; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008827; Chromosome 5.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
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; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 2: Evidence at transcript level;
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:UP000008827}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 809 AA; 91361 MW; DF574FB6023B8E88 CRC64;
MYVVKRDGRQ ETVHFDKITA RLKKLSYGLS TEHCDPVLVS QKVCAGVYKG VTTSQLDELA
AETAAAMTAN HPDYASLAAR IAVSNLHKNT KKSFSETIKV MYYHFNERSA MKAPLIADDV
YEIIIKNAAR LDSEIIYDRD FDYDYFGFKT LERSYLLKVQ GKVVERPQHM LMRVAVGIHK
DDIDSAVRTY HMMSQRWFTH ASPTLFNAGT PRPQLSSCFL VCMKDDSIEG IYDTLKECAV
ISKSAGGIGV SVHNIRATGS YIRGTNGTSN GIVPMLRVFN DTARYVDQGG GKRKGAFAVY
LEPWHADIFE FLDLRKNHGK EEHRARDLFY ALWVSDLFME RVQSNGQWSL FCPNEAPGLA
DCWGEEFEKL YTQYEREGKA KKVVQAQNLW FEILKSQIET GTPYMLFKDT CNKKSNQQNL
GTIKSSNLCT EIIEYTSPTE TAVCNLASIA LPRYVREKGV PMESHPSKLV GSRGSKNRYF
DFDKLGEVTA IVATNLNKII DVNYYPVDTA RRSNMRHRPI GIGVQGLADT FILLGVAFDS
PEAQQLNKDI FETIYYHALK TSSELAAKEG PYETYSGSPI SKGILQPDMW GVMPSSRWDW
DALREMIAKT GVRNSLLVAP MPTASTSQIL GNNECFEPYT SNIYSRRVLS GEFVVVNKHL
LHDLTEMGLW SPTIKNNIIY EDGSVQKIPE IPDDLKIIYK TVWEIKQKTL VDMAVDRGCY
IDQSQSLNIH MDQPNFGKLT SLHFYAWSKG LKTGMYYLRS RAAADAIKFT VDTSMLHEKP
MAEEEDDNTK MAQMVCSLTN REECLACGS
//
