ID A0A1I0YS94_9FLAO Unreviewed; 807 AA.
AC A0A1I0YS94;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05660845_1879 {ECO:0000313|EMBL:SFB15178.1};
OS Flavobacterium swingsii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=498292 {ECO:0000313|EMBL:SFB15178.1, ECO:0000313|Proteomes:UP000199604};
RN [1] {ECO:0000313|EMBL:SFB15178.1, ECO:0000313|Proteomes:UP000199604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21789 {ECO:0000313|EMBL:SFB15178.1,
RC ECO:0000313|Proteomes:UP000199604};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJT01000004; SFB15178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0YS94; -.
DR STRING; 498292.SAMN05660845_1879; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000199604; 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}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 807 AA; 91510 MW; A5A771676E143D51 CRC64;
MYVVKRDGHK EPVMFDKITE RIKKLCYGLN DLVDAVKVAM RVIEGLYDGV STSELDNLAA
ETAASMTIAH PDYAQLAARI AISNLHSNTN KSFSETMNEM YHYVNPRNGQ EAPLLSEEVH
NVIQENAEFL NSHIIYTRDF NYDYFGFKTL ERSYLLKING KIVERPQHML MRVSVGIHLN
DLKSVIETYD LMSKKFFTHA TPTLFNAGTP KPQMSSCFLL AMQDDSIDGI YDTLKQTAKI
SQSAGGIGLS IHNVRATGSY IRGTNGTSNG IVPMLRVFND TARYVDQGGG KRKGSFAIYI
ETWHADIFDF LDLKKNTGKE EMRARDLFFA MWTSDLFMKR VEENGNWTLM CPNECPGLYD
VHGEEFEALY TSYEAAGKGR KTIKAHELWE KILESQIETG TPYMLYKDAA NRKSNQKNLG
TIRSSNLCTE IMEYTSKDEI AVCNLASLSL PMFVEGGKFN HDLLFTVTKR VTRNLNKVID
RNYYPVIEGE NSNKRHRPIG LGVQGLADAF IMLRLPFTSD EAKKLNEEIF ETLYFAAVTA
SMEMAIEEGP YSTFAGSPIS QGEFQYNLWG LKDEDLSGRW DWASLRKEVM KNGVRNSLLV
APMPTASTSQ ILGNNEAFEP YTSNIYTRRV LSGEFIVVNK HLLEDLVKLG LWTEDLKQQL
MRENGSVQNL DIPQDLKDLY KTVWEMSMKD IIDMSRHRGY FVDQSQSLNL FMQDANYSKL
TSMHFYAWKS GLKTGMYYLR TKAAVDAIKF TLNNDKKAEP IAAIEVKEQP VLAEVEVVTT
AMTNEEYRAM IELAKNAGPE DCEMCGS
//
