ID   A0A0C5WC70_9FLAO        Unreviewed;       829 AA.
AC   A0A0C5WC70;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=AW14_04115 {ECO:0000313|EMBL:AJR02944.1};
OS   Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Siansivirga.
OX   NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR02944.1, ECO:0000313|Proteomes:UP000032229};
RN   [1] {ECO:0000313|EMBL:AJR02944.1, ECO:0000313|Proteomes:UP000032229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR02944.1,
RC   ECO:0000313|Proteomes:UP000032229};
RA   Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL   Submitted (FEB-2014) 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|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|ARBA:ARBA00000206,
CC         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; CP007202; AJR02944.1; -; Genomic_DNA.
DR   RefSeq; WP_044637643.1; NZ_CP007202.1.
DR   AlphaFoldDB; A0A0C5WC70; -.
DR   STRING; 1454006.AW14_04115; -.
DR   KEGG; sze:AW14_04115; -.
DR   PATRIC; fig|1454006.5.peg.799; -.
DR   HOGENOM; CLU_000404_1_0_10; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000032229; Chromosome.
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:UP000032229}.
FT   DOMAIN          1..91
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   829 AA;  93864 MW;  93239168E1154262 CRC64;
     MYVVKRGGRK EQVMFDKITA RVRKLCYGLN ELVDPLKVTM RVIEGLYDGV TTSELDNLAA
     EIAATMTTAH PDYARLAARI SVSNLHKNTK KTFSEVMHDL YTYVNPRTGK NAPLLADDVY
     EVIMENKDVL DSTIIYNRDF GYDYFGFKTL ERSYLLKLNG EIAERPQHML MRVAVGIHLN
     DLESVIETYE LMSKKYFTHA TPTLFNSGTP KPQMSSCFLL TMKDDSIDGI YDTLKQTAKI
     SQSAGGIGLA IHNIRATGSY IAGTNGTSNG IVPMLKVFND TARYVDQGGG KRKGSFAMYI
     ETWHADIMDF LDLKKNHGKE EMRARDLFYA MWISDLFMER VQEDGPWTLM CPNECPGLDE
     VHSEAFEALY LKYEAEGKGR KTIKARELWE KILESQIETG TPYMLYKDAA NRKSNQQNLG
     TIRSSNLCTE ILEYTSPDEV AVCNLASIAL PMFVKNGEFD HKELFRITKR VTKNLNRVID
     RNYYPVVEAK NSNMRHRPIG LGVQGLADTF IQLRMPFTSD QAKKLNQDIF ETLYYAAVTA
     SMEEAKADGP YQTYEGSPIS KGQFQHNLWN IKDEELSGNW DWDKLRKQVL KHGVRNSLLV
     APMPTASTSQ ILGNNECFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVELG LWNDGLKQDI
     MRANGSVQNV DVPQHIKDLY KTVWELSMKD IIDMSRQRGY FIDQSQSLNL FMEGATMAKL
     TSMHFYAWKS GLKTGMYYLR TKSAVDAIKF TLSTTKKEEP TAEEVVVVNE ADSAKQEQKR
     QIAVNNAAKF AQQTNTAESN VEPMTAEEMK ALIAQAKASE GDDCLMCGS
//