ID A0A068UWP9_COFCA Unreviewed; 808 AA.
AC A0A068UWP9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=GSCOC_T00037524001 {ECO:0000313|EMBL:CDP12851.1};
OS Coffea canephora (Robusta coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=49390 {ECO:0000313|EMBL:CDP12851.1, ECO:0000313|Proteomes:UP000295252};
RN [1] {ECO:0000313|Proteomes:UP000295252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX PubMed=25190796; DOI=10.1126/science.1255274;
RA Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA Lashermes P.;
RT "The coffee genome provides insight into the convergent evolution of
RT caffeine biosynthesis.";
RL Science 345:1181-1184(2014).
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; HG739155; CDP12851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068UWP9; -.
DR STRING; 49390.A0A068UWP9; -.
DR EnsemblPlants; CDP12851; CDP12851; GSCOC_T00037524001.
DR Gramene; CDP12851; CDP12851; GSCOC_T00037524001.
DR InParanoid; A0A068UWP9; -.
DR OMA; QMSSCYL; -.
DR PhylomeDB; A0A068UWP9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000295252; Chromosome 7.
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; 1.
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:UP000295252}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 808 AA; 90988 MW; F6F506262BA3BB21 CRC64;
MYVVKRDGRQ EAVHFDKITA RLKKLSYGLS SDHCDPVLVS QKVCAGVYKG VTTSQLDELA
AETAAAMTAN HPDYASLAAR IAVSNLHKNT KKSFSETVKD MYGHVSERSG LKAPLIADDV
YEIIMKNAAR LDSEIIYDRD FDYDYFGFKT LERSYLLKVQ GKVVERPQHM LMRVAVGIHK
DDIDSALRTY HLMSQRWFTH ASPTLFNAGT PRPQLSSCFL LCMKEDSIEG IYDTLKECAV
ISKSAGGIGV SVHNIRATGS YIRGTNGTSN GIVPMLRVFN DTARYVDQGG GKRKGAFAVY
LEPWHADIFE FLDLRKNHGK EEHRARDLFY ALWVPDLFME RVQKNEQWTL FCPNEAPGLA
DCWGTEFERL YTQYEKQGKA KKVVQAQNLW FEILKSQIET GTPYMLYKDT CNRKSNQQNL
GTIKSSNLCT EIIEYTSPTE TAVCNLASIA LPRYVREKGF TSESQPSKLV GSRGSANRFF
DFDKLAEVTA IVTSNLNKII DINYYPVDTA KRSNFRHRPI GIGVQGLADT FILLGMAFDS
PEAQQLNKDI FETIYYYALK SSSELAAKDG PYETYDGSPV SKGILQPDMW GVTPSSRWDW
DALRAMIATN GVRNSLLIAP MPTASTSQIL GNNECFEPYT SNIYSRRVLS GEFVVVNKHL
LHDLTEMGLW TPALKNRIIY EDGSVQKIPE IHEDLKAIYK TVWEIKQRTL VDMAVDRGCY
IDQSQSLNIH MDQPNFGKLT SLHFHAWSKG LKTGMYYLRS RAAADAIKFT VDTAMLKDKP
KTTADDDSKM AQMVCSLANR EECMACGS
//
