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Database: UniProt
Entry: A0A1Z5JAQ3_FISSO
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ID   A0A1Z5JAQ3_FISSO        Unreviewed;       800 AA.
AC   A0A1Z5JAQ3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=FisN_2Lh595 {ECO:0000313|EMBL:GAX11074.1};
OS   Fistulifera solaris (Oleaginous diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC   Fistulifera.
OX   NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX11074.1, ECO:0000313|Proteomes:UP000198406};
RN   [1] {ECO:0000313|EMBL:GAX11074.1, ECO:0000313|Proteomes:UP000198406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX11074.1,
RC   ECO:0000313|Proteomes:UP000198406};
RX   PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA   Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA   Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA   Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT   "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT   by the genome and transcriptome.";
RL   Plant Cell 27:162-176(2015).
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {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:GAX11074.1}.
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DR   EMBL; BDSP01000035; GAX11074.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5JAQ3; -.
DR   InParanoid; A0A1Z5JAQ3; -.
DR   OrthoDB; 5472715at2759; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000198406; 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:UP000198406}.
FT   DOMAIN          1..92
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   800 AA;  89835 MW;  1DC4AED5AF350E94 CRC64;
     MYVLKRNGKR ESVHFDKITS RVSKLCYGLD AKHVDPVVIS QKVIQGVYPG VTTCELDELA
     AQTAAAMATQ HPDYSILAAR ISVSNLHKMT VARFSELCQL FHDYKHPQTG EPAPLISQEV
     YDISQKYAGE LDGAIVHARD FEYDYFGFKT LEKSYLLKMH GQIAERPQLL LMRVAVGIHG
     DDIPKVIETY NDLSNRYFTH ATPTLFNAGT NMPQMSSCFL LTMKQDSIEG IYDTLKNCAI
     ISKYAGGIGL AIHNIRASKS YIRGTNGTSN GIVPMLRVFN NTARYVDQGG GKRKGSIACY
     LEPWHADVFE FLDLRKNHGN ESDRARDLFY ALWVPDLFMK RVKENSTWSL FCPNEAPGLA
     DCYGAEFEAL YEKYEQEGRA RQTIKAQTLW FAILDSQVET GTPYILYKDA CNEKSNQKNL
     GTIRCSNLCT EIVEYTAPDE TAVCNLASIS LSKLVTPTTD AEEGSFDFDR LNEISQVVTR
     NLNKIIDRNY YPIEEARNSN MRHRPIGIGV QGLADAFQML RLPFDSPQAR QLNKDIFETI
     YYGACCASCE LAEIDGPYST YVGSPASQGQ LQFDLWGVTP SDRWDWAALK ERIAQHGLRN
     SLLLAPMPTA STAQILGNNE STEPFTSNMY NRRVLAGEFT VVNKHLLREL TARGLWNEDV
     RNRIIADNGS IQNVKSIPES IRDVYKTVWE IPQRSILDMA AERAPYICQS QSLNVHLAEP
     DSKKLTSMHF YAWKKGLKTG MYYLRTRPKA DAIKFTVDQE LINADKQKKA QTGAKPVNGF
     QGAAGLTTVN DEEECLNCGA
//
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