ID A0A2I0SWF6_9ACTN Unreviewed; 793 AA.
AC A0A2I0SWF6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CW362_04845 {ECO:0000313|EMBL:PKT74278.1};
OS Streptomyces populi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT74278.1, ECO:0000313|Proteomes:UP000236178};
RN [1] {ECO:0000313|EMBL:PKT74278.1, ECO:0000313|Proteomes:UP000236178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A249 {ECO:0000313|EMBL:PKT74278.1,
RC ECO:0000313|Proteomes:UP000236178};
RA Wang Z.;
RT "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT isolated from stems of Populus adenopoda Maxim.";
RL Submitted (DEC-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}.
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:PKT74278.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PJOS01000005; PKT74278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0SWF6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000236178; 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; 3.20.70.20; -; 1.
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; 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; 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:UP000236178}.
FT DOMAIN 589..611
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87113 MW; 735EFFD79A51D40F CRC64;
MTIAPADPAS ATAQQAPVET DGPGTALLRT LTDLTADLPD ADPGRVAAAA LRGRSARADE
AELRELATEA AAGLISEDPA YSRLAARLLA ITIAAEAASQ GVTAFSESVA VGHREGLIAD
RTAAFVRLHT ARLDALIDAE GDDRFGYFGL RTLHSRYLLR HPITRKVVET PQHFMLRVAS
GLAEDDTVRS VDEVAALYRL MSRLDYLPSS PTLFNSGTRH PQMSSCYLLD SPLDELDSIY
DRYHQVARLS KHAGGIGLSY SRIRSRGSLI RGTNGHSNGI VPFLKTLDAS VAAVNQGGRR
KGAAAVYLET WHSDIEEFLE LRDNTGEDAR RTHNLNLAHW IPDEFMRRVN ADGVWSLFSP
ADVPELVDLW GDEFDAAYRK AEEAGLARKT IPARDLYGRM MRTLAQTGNG WMTFKDAANR
TANQTAEPGH TVHSSNLCTE ILEVTDDGET AVCNLGSVNL GAFVTGGDID WERLDETVRT
AVTFLDRVVD INFYPTEQAG RSNAKWRPVG LGAMGLQDVF FKLRIPFDSP EARALSTRIA
ERIMLASYEA SADLAERNGP LPAWEKTRTA RGVLHPDHFD VELNWPERWA ALRERIASVG
MRNSLLLAIA PTATIASIAG VYECIEPQVS NLFKRETLSG EFLQVNSYLV AELKELGVWD
AQTREALRES NGSVQGFTWV PQEVRDLYRT AWEIPQRGLI DMAAARTPFL DQAQSLNLFL
ETPTIGKLSS MYAYAWKAGL KTTYYLRSRP ATRIARAAQA QARPETTIPV QQAADPDAVA
CSLENPESCE ACQ
//
