ID A0A2U1JK69_9FLAO Unreviewed; 803 AA.
AC A0A2U1JK69;
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=DB895_06075 {ECO:0000313|EMBL:PWA05551.1};
OS Flavobacterium psychrotolerans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2169410 {ECO:0000313|EMBL:PWA05551.1, ECO:0000313|Proteomes:UP000245449};
RN [1] {ECO:0000313|EMBL:PWA05551.1, ECO:0000313|Proteomes:UP000245449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB1R5 {ECO:0000313|EMBL:PWA05551.1,
RC ECO:0000313|Proteomes:UP000245449};
RA Liu Q., Xin Y.-H.;
RT "Flavobacterium sp. nov., isolated from glacier ice.";
RL Submitted (APR-2018) 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}.
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:PWA05551.1}.
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DR EMBL; QCZI01000006; PWA05551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1JK69; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000245449; 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:UP000245449}.
FT DOMAIN 1..91
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 803 AA; 91285 MW; 3BC5A5D6F4732593 CRC64;
MYVVKRDGRK EPVMFDKITD RIKKLCYGLN DLVDAVKVAM RVIEGLYDGV STSELDNLAA
ETAASMTIAH PDYAQLAARI AISNLHSNTN KSFSETMNDM FHYVNPRNGQ DAPLLSEEVH
AVIMENAEFL NSHIIYNRDF NYDYFGFKTL ERSYLLKING KIVERPQHML MRVSVGIHLN
DLKSVIETYD LMSKKFFTHA TPTLFNAGTP KPQMSSCFLL AMKDDSIDGI YDTLKQTAKI
SQSAGGVGLS IHNIRATGSY IRGTNGTSNG IVPMLRVFND TARYVDQGGG KRKGSFAIYI
ETWHADIFEF LDLKKNTGKE EMRARDLFFA MWTSDLFMKR VQEDSYWTLM CPNECPGLYD
VYGEEFEALY TDYEERGKGR KTIKAHELWE KILESQIETG TPYMLYKDAV NRKSNQKNLG
TIRSSNLCTE IMEFTSKDEV AVCNLASISL PMFVENKKFN HKLLYTVTKR VTRNLNKVID
RNYYPVIEGE NSNKRHRPIG LGVQGLADAF ILLRLPFTSD EAKKLNQEIF ETLYFAAVTA
SMEMAKEEGP YSSFVGSPIS QGEFQYNLWG LKDEELSGRW DWASLRKEVM KHGVRNSLLV
APMPTASTSQ ILGNNEAFEP YTSNIYTRRV LSGEFIVVNK HLLNDLVELG LWNETLKQEL
MRNNGSVQDL NIPQDLKDLY KTVWEMSMKD IIDMSRQRGY FVDQSQSLNL FMQNANYSKL
TSMHFYAWQS GLKTGMYYLR TKAAVDAIKF TLNNDKKTEP IAAVAAVAVA VEAAPQEMSA
DEYRALIELS RNADAEDCEM CGS
//
