ID   A0A1L0BZV3_9ASCO        Unreviewed;       881 AA.
AC   A0A1L0BZV3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMEA4029010_CIC11G00000004480 {ECO:0000313|EMBL:SGZ55954.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ55954.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ55954.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ55954.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|RuleBase:RU003410};
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|RuleBase:RU003410}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT635760; SGZ55954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0BZV3; -.
DR   STRING; 45354.A0A1L0BZV3; -.
DR   OrthoDB; 5472715at2759; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000182334; Chromosome v.
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:SF28; 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:UP000182334}.
FT   DOMAIN          591..613
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   881 AA;  99760 MW;  DE435CC803EC4BCD CRC64;
     MTIVENETGT HGPFEADRFR TLLEKLSGTL TISADKMDSL VHDIEASLPE SLLFNQLIEL
     AAESVALRTI INPDCGLLAG RLEAYRIRRL VPKRFSEAFR TLRLNHHTRT RQPYPLVSKA
     AAEIVESNAD YLDSLVCPER DFDLSYFGVR TLQKSFLLHI DKVVAETPQY LFLRVAVGIH
     GIHGDADMLA RIKETYDLMS SKYMIHSSPT LFNAGTDNNF LSLCYLMATE DDSIDGIYKT
     LHKAAMISKG SGGIGIHVSN VRACGALIKA SNGTSGGLVP MLRVFNNTAR YVDQGGNKRP
     GAMAVYLEPW HADVQEVLEL RKNHGQEELR ARDLFYALWI PDLFMKRVKE NEDWSLFSPD
     EAPGLNDVFG QEFEDKYTLY ERQGLAMQTI KARKLWMQIL ESQTETGMPF MLYKDSCNRK
     LNQKNLGTIK SSNLCCEIVE YSSPEEIAVC NLGLLALPSF VNAGHENGIY FDFPKLHQVT
     KVLARNLDKV IDVTKYPVDI SETSNKRHRP IAIGVQGLAD TFLELRLPFE SEKARKLNSQ
     IFETIYHAAV ECSVEMAIEK GAYESFEGSP ASMGKLQFDL WNHKPRFFDD WDVLKERVKI
     YGLRNSLLVA PMPTATTSQI LGFNECFEPF TSNLYLRRVL SGEFQVVNKY LVKDLEDMGI
     WSDALKNAII KDNGLIQKID IIPSEIKELY KTVWEISQKV VVQLAADRGR FIDQLQSMNI
     HLQNPTFKTL TSCHFYAWEQ GLKTGMYYLR TQAASRAIQF TIDEAKIKAS LDSITGKKIA
     SLKRREYIEA NGYPKKEAGQ TSQEFYKRLA ESTPCSITSY ESDKERDMLL KHAISRSHKK
     RRKVVNGDRN GENQDETYDI YDETPLSCNI SDVEGCEACS G
//