ID A0A2U2PHF3_9SPHI Unreviewed; 696 AA.
AC A0A2U2PHF3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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=DDR33_10300 {ECO:0000313|EMBL:PWG80836.1};
OS Pararcticibacter amylolyticus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pararcticibacter.
OX NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG80836.1, ECO:0000313|Proteomes:UP000245647};
RN [1] {ECO:0000313|EMBL:PWG80836.1, ECO:0000313|Proteomes:UP000245647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG80836.1,
RC ECO:0000313|Proteomes:UP000245647};
RA Cai Y.;
RT "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
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:PWG80836.1}.
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DR EMBL; QEAS01000007; PWG80836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2PHF3; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000245647; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000245647}.
FT DOMAIN 554..576
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 696 AA; 80015 MW; 4FD8B802A8993749 CRC64;
MIAKKWILLN NEIMMKQDDG FSLDKDKEAV RSYFLDYVNK NTVFFYTLKE KIDYLIENHY
YINFYEWYTF DQMKAVYDLV YSRKFRFPSF MSAFKFFQSY ALRDDSGEKF LERYEDRLAV
IALFLARGDV NQALENAEML INQEYQPATP TFLNAGKKRS GELVSCFLDE VGDNLNGIGY
AIDSAMKLSS IGGGVSFNMS KVRGRGESIK GVENLASGVL PVMKIMEDTF SYANQLGQRP
GAGAVYLNVF HSDIEEFLDC KKINVDEKVR IKTLSIGVVI PDKFMELAEK DEPCYLFYPH
TVKLEYGQYL DELDMDGMYE ELITNPKIRK KKVNARHLLV KIAQTQKESG YPYLFFKNNA
NRQHALNGIG NVKFSNLCTE IMQVSDVSDI GSYGQEDTIR YGISCNLGSL NIVTVMENKR
IKEAVKTAMT TLTVVSDNTN ISMVPSIRKA NEELHSVGLG AMNLHGFLAK NFMMYESEEA
LDFCNVFFMM VNFYSLERSM EIARDRKTTF KGFEHSAYAS GEYFEKYIRE DIYPQSETVK
QLFEGIEIPG KEAWAQLKQQ VAEHGIYHAY RMAIAPNQST SYIMNSTASV MPVVDVIEVR
EYGDSTTYYP MPYLTNDNYF FYKSAYDMDQ KKILRLISVI QRHVDQGIST ILHTNSRDTT
RDLSVYYIYA HKMGLKSLYY TRTRKASIDE CVSCAV
//
