ID Q6BZQ3_YARLI Unreviewed; 892 AA.
AC Q6BZQ3;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 125.
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=YALI0_F31735g {ECO:0000313|EMBL:CAG78922.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG78922.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG78922.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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; CR382132; CAG78922.1; -; Genomic_DNA.
DR RefSeq; XP_506109.1; XM_506109.1.
DR AlphaFoldDB; Q6BZQ3; -.
DR STRING; 284591.Q6BZQ3; -.
DR EnsemblFungi; CAG78922; CAG78922; YALI0_F31735g.
DR GeneID; 2908285; -.
DR KEGG; yli:YALI0F31735g; -.
DR VEuPathDB; FungiDB:YALI0_F31735g; -.
DR HOGENOM; CLU_000404_1_0_1; -.
DR InParanoid; Q6BZQ3; -.
DR OMA; RGSIQNI; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001300; Chromosome F.
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:UniProtKB-UniPathway.
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:UP000001300}.
FT DOMAIN 4..95
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 818..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 100993 MW; CB05C3C8A9FA7735 CRC64;
MSKLFVIKRD GRKESVQVDK ITARIKRLCY GLDPDHVDPI QITLKIASGI YEGVSTIELD
NLAAETAAYM TTLHPDYAIL AARIAVSNLH KQTKKQFSQV VYDLYHYVNP RNKKHSPMVS
KELYDTVQAN ADELNGAILY DRDFTYNYFG FKTLERAYLL RVNGAVAERP QQMIMRVSVG
IHGDNIARAI ETYNYMSQKY FTHASPTLYN AGTPQPQMSS CFLVNMKDDS IDGIYDTLKT
CALISKSAGG IGLSIHNIRA TGSYIAGTNG TSNGIVPMLR VYNNTARYVD QGGNKRPGAF
AMYLEPWHDD IFEFCELRKN HGKEEIRARD LFLALWIPDL FMERVEQNAE WTLMCPNECP
GLDDVYGDEF KQLYEQYEKE GRGRRTIPAQ KLWYHILDCQ TESGNPFMLY KDSCNRKSNQ
KNLGTIKSSN LCCEIVEYSS PDEVAVCNLA SIALPTFVTR DDTNSFYDFK KLHDIAKVIV
RNLNAIIDRN YYPVPEAKKS NMRHRPIALG VQGLADTFMA LRLPFESEEA KKLNIQIFET
IYHGAVEASY EMALEDGAYE TFQGSPASKG DLQFDLWNVT PSELWEWDDL KAKIMKTGMR
NSLLVAPMPT ASTSQILGFN ECFEPYTSNI YSRRVLAGEF QIVNPWLLKD LVEVGLWNET
MKNRIVADNG SVQNIPNIPQ EIKDLYKTVW EISQKRIIEM AADRSPFIDQ SQSLNIHIKD
PTMGKLTSMH FYGWKKGLKT GMYYLRTMAA AAPIQFTIDQ EALKTIDSST AKAMLNKKPY
QEINSMANLR SIEDKIAKID LNGGNKENNV MELIRESQEK KEAEKEAKRV PAPVAETKEE
TQEETKPVEK PAAAEDKPAE DSPIAKSEYD IYADKVLACS LANPESCEMC SG
//