ID   A0A2S1LK89_9FLAO        Unreviewed;       794 AA.
AC   A0A2S1LK89;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=FK004_02320 {ECO:0000313|EMBL:AWG24138.1};
OS   Flavobacterium kingsejongi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1678728 {ECO:0000313|EMBL:AWG24138.1, ECO:0000313|Proteomes:UP000244677};
RN   [1] {ECO:0000313|EMBL:AWG24138.1, ECO:0000313|Proteomes:UP000244677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ004 {ECO:0000313|EMBL:AWG24138.1,
RC   ECO:0000313|Proteomes:UP000244677};
RA   Lee P.C.;
RT   "Complete genome sequence of Flavobacterium kingsejong AJ004.";
RL   Submitted (APR-2017) 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; CP020919; AWG24138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S1LK89; -.
DR   KEGG; fki:FK004_02320; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000244677; 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:UP000244677}.
FT   DOMAIN          1..91
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   794 AA;  90368 MW;  6416033EDA16C71D CRC64;
     MFVVKRDGNR EPVMFDKITD RVKKLCYGLN DLVDPVKVAM RVIEGLYDGV TTSELDNLAA
     ETAASMTISH PDYAQLAARI AVSNLHKNTK KSFSETMTDM YHYVNPRTGK EAPLLADDVF
     EIIQKNAQVL DSTIIYNRDF NYDYFGFKTL ERSYLLKING KIVERPQHML MRVSVGIHKD
     DIESVIETYE LMSKKFFTHA TPTLFNSGTP KPQMSSCFLL TMKDDSIDGI YDTLKQTAKI
     SQSAGGIGLA IHNVRATGSY ISGTNGTSNG IVPMLRVYDM TARYVDQGGG KRKGSFAIYV
     EPWHADIFDF LDLRKNHGKE EMRTRDLFLG MWIPDLFMKR VQEDSTWTLM CPNECPGLSE
     VHSEEFDALY LRYEAEGKGR KTIKAREIWE KILESQVETG LPYMLYKDAA NRKSNQKNLG
     TIRSSNLCTE IIEYTSPDEV AVCNLASISL PMFVENGKFD HKKLFDVTKR VTLNLNKVID
     RNYYPVIEAE NSNVRHRPVG LGVQGLADAF IMLRMPFTSD EAKKLNQEIF ETLYFAAVTA
     SMELSKIEGP YSTFKGSPIS QGEFQYNLWG LKDEELSGRW DWTSLRKEVM EHGVRNSLLV
     APMPTASTSQ ILGNNEAFEP YTSNIYTRRT LSGEFIVVNK HLLEDLVDLG LWNETLKQEI
     MRHNGSVQNI DVIPAHIKEL YKTVWEMSMK DILDMSRQRG YFIDQSQSLN LFMENANFAK
     LTSMHFYAWQ SGLKTGMYYL RTKSAVDAIK FTLNNDKKEQ PVALETEEIA VEDFKAMLLK
     AQASEPDDCE MCGS
//