ID A0A0R3PMA1_ANGCS Unreviewed; 795 AA.
AC A0A0R3PMA1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU003410};
GN ORFNames=ACOC_LOCUS5994 {ECO:0000313|EMBL:VDM57579.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000599301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000599301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM57579.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM57579.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-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|ARBA:ARBA00024942,
CC 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}.
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DR EMBL; UYYA01003911; VDM57579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3PMA1; -.
DR STRING; 334426.A0A0R3PMA1; -.
DR WBParaSite; ACOC_0000599301-mRNA-1; ACOC_0000599301-mRNA-1; ACOC_0000599301.
DR OMA; QMSSCYL; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; 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; 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:UP000267027}.
FT DOMAIN 7..98
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 795 AA; 90114 MW; DF960F354DF28701 CRC64;
MQRHNSTYVV KRDGRKEGVH FDKITARILK LSYNLNMDYV DPVLVAMKVI AGLYKGVTTV
ELDNLAAETA ASMTTKHPDY AILAARIAVS NLHKKTGKVF SEVMQKLYEF RHPSTGEHCP
MISKETCDII MKHADVLNSA IVYDRDFSYT YFGFKTLERS YLLKMNKEVA ERPQHMLMRV
AVGIHGEDID AAIETYNLMS ERYFTHASPT MFNAGTLWPQ LSSCFLLTMS EDSIAGIYDT
LKQCALISKS AGGIGLNVHK IRATGSLIGG TNGTSNGLVP MLRVYNNTAR YVDQGGNKRP
GAFAIYLEPW HADIFEFVAL KRNTGPEEER ARDLFYALWI PDLFMKRVER DMEWSLMCPH
ECPGLDDCWG EKFDELYTRY EAEGRYRKRV KARKLWEHIV SSQIETGTPY IVYKDACNRK
SNQQNLGTIK CSNLCTEIVE YSSKDEIAVC NLGSVALNRF VTAEKKFDFA KLKEVTKVLT
YNLNKIIDIN YYPVEEARRS NFRHRPIGIG VQGLADAFML MRYPFTSPEA RDLNKRIFET
IYYAALEASC ELAEKHGTYE TYEGSPVSKG ILQFDMWNVT PTDQCDWDCL REKIKTHGVR
NSLLLAPMPT ASTAQILGNN ESIEPYTSNI YSRRVLSGDF QIVNPHLLKD LVELNLWDDE
IKNQLIANNG SIAKIGGIPD NIKQLYQTVW ELPQKDIIEM AADRGAFIDQ SQSLNIHIAR
PSYANITSMH FYGWKKGLKT GMYYLRTKPA VNAVQFTVDK EALRAKEERD AMLNNVASKI
ASVNVGDEGC LMCSG
//
