ID Q6BJ31_DEBHA Unreviewed; 867 AA.
AC Q6BJ31;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
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 OrderedLocusNames=DEHA2G05610g {ECO:0000313|EMBL:CAG90249.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG90249.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG90249.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
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 -!- 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; CR382139; CAG90249.1; -; Genomic_DNA.
DR RefSeq; XP_461790.1; XM_461790.1.
DR AlphaFoldDB; Q6BJ31; -.
DR STRING; 284592.Q6BJ31; -.
DR GeneID; 2904667; -.
DR KEGG; dha:DEHA2G05610g; -.
DR VEuPathDB; FungiDB:DEHA2G05610g; -.
DR eggNOG; KOG1112; Eukaryota.
DR HOGENOM; CLU_000404_1_2_1; -.
DR InParanoid; Q6BJ31; -.
DR OMA; QMSSCYL; -.
DR OrthoDB; 5472715at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000599; Chromosome G.
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:UP000000599}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 784..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 97369 MW; 5276DCAB77BCBB49 CRC64;
MYVYKRDGRK EPVRFDKITA RVQRLCYGLD TTHVEPVAIT QRVISGVYQG VNTIELDNLA
AETAAYMTTI HPDYAILAAR IAVSNLHKQT TKQFSQVSKE LYEYVNPKTD LHSPMISKDT
YDIIQANANE LNSAIVFDRD FNYNYFGFKT LERSYLLRIN GKVAERPQHL IMRVAVGIHG
NDIERVIESY NMMSLRYFTH GSPTLFNAGT PSPQMSSCFL VAMKDDSIDG IYDTLKTCAL
ISKSAGGIGL HIHNIRSTGA YIAGTNGTSN GIIPMVRVFN NTARYVDQGG NKRPGAFALY
LEPWHADIFD FIDIRKNHGK EEIRARDLFP ALWIPDLFMK RVEQNGDWTL FSPNEAKGLS
DVYGDEFEEL YTKYEKENRG RSVVKAQKLW YAILDAQTET GTPFMLYKDA CNKKTNQKNL
GIIKSSNLCC EIVEYSAPDE VAVCNLASIA LPAFVDKNNT TSWYDFEKLH EVTKVVTRNL
NRIIDRNYYP VPEARNSNMR NRPIALGVQG LADAFMALRL PFDSQEAKEL NTQIFETIYH
GAVEASIELA EIEGPYQTYE GSPASKGILQ FDLWERKPTE LWDWDTLKQK LAKHGIRNSL
LVAPMPTAST SQILGYNECF EPYTSNIYSR RVLAGEFQIV NPYLLRDLVD LGIWNDDMKN
NIISNNGSIQ TLPNIPDELK ALYKTVWEIS QKHIIDMAAD RAAFIDQSQS LNIHIKDPTM
GKLTSMHFYG WKKGLKTGMY YLRTQAAAAA IQFTVDQNSV NNASKTIASL EKLNQRKYIA
KSVSSTNDSG VSTEPTSLEN SVADLKISDN SNTPKNDNPV ESTESTESTE STESTEPAEG
QDAGDIYSSK VIACAIDNPE SCTMCSG
//
