ID A0A409Y1Z3_9AGAR Unreviewed; 728 AA.
AC A0A409Y1Z3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CVT26_001246 {ECO:0000313|EMBL:PPQ97064.1};
OS Gymnopilus dilepis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ97064.1, ECO:0000313|Proteomes:UP000284706};
RN [1] {ECO:0000313|EMBL:PPQ97064.1, ECO:0000313|Proteomes:UP000284706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRW20 {ECO:0000313|EMBL:PPQ97064.1,
RC ECO:0000313|Proteomes:UP000284706};
RX PubMed=30283667; DOI=10.1002/evl3.42;
RA Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA Matheny P.B., Slot J.C.;
RT "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT diversity.";
RL Evol. Lett. 2:88-101(2018).
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|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:PPQ97064.1}.
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DR EMBL; NHYE01001295; PPQ97064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A409Y1Z3; -.
DR STRING; 231916.A0A409Y1Z3; -.
DR InParanoid; A0A409Y1Z3; -.
DR OrthoDB; 1662144at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000284706; Unassembled WGS sequence.
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 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; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 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.
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:UP000284706}.
FT DOMAIN 110..181
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 196..713
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 728 AA; 80924 MW; 4D158424AF42B5E5 CRC64;
MRDEEKAVVD VTRILDDVMK AAQPVITATE LDALLASITA RLSHVHPAYE KVAGRMAMGA
LYKDTPSSFT DSVKLSFKDH STFFTTMYRQ SVNALAPFLD AEIISERDFD LTYDAVLLFR
DVYLLRRAGK VLERPQHLYL RISIAINGPN LNAVRKTYGH LSKGLYIHEP SAMMYAGTTL
GQMIPRYSLP FDGRSSMDKF MKLTECSMIS YAGGSVSLSV SDFPAEGELV EGQPSGGLPA
ITRVFDSVIH RIGKGGDLIR GKITMYMEPW HSEIFQFLQS NMTVFAERLT EARGLFFAMW
IPDLFLHRVE QGGNWSLFRP GDVPLLTNVW GAEFDDVYRM YEGRRIAVKS LPAKELWDVI
LNGIMETGGP SIMFKDAANS KSNLAHIGRL THGGPAADTA LFSSSCETGV SATASIVLPT
FVSVDGTFNY QLLHRIAKSV TRDLNRVLLL NNYPSMPTAA SYVLHRSIGI GIVGLADTFI
SLRIPFDSED AIRIGGLIME TIYHASLQMS CDLVDLYGAY PTFTGSPLSR GRFQFNLWDV
DVSSSRYDWN ALRSRIMQRG VVNAQVVLLS DTTSSSRLTS CSEGFEPILR RVNAINSTVL
VKGIASTSYI APNVSLVSEL QKLGLWDDAM RHDLLSSCGS VQAIDRIPMN LKNIFKTAWE
VQQEVIIRHA VARAPFVCHS QSIMMYRDGP ARHWLSVCLF LAWKEGLKTG IYVLRGRPSY
SNRAVYPA
//