ID A0A345XIP5_9ACTN Unreviewed; 796 AA.
AC A0A345XIP5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DVA86_01460 {ECO:0000313|EMBL:AXK31511.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK31511.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK31511.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK31511.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-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}.
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DR EMBL; CP031320; AXK31511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XIP5; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000254425; Chromosome.
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:UP000254425}.
FT DOMAIN 596..618
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 86352 MW; 2E78B26AB32503A1 CRC64;
MTTAPAAAAA TAPSAPPAAR TDPGAAALTR LLTGLAADLP ATDPHRVAAA ALRGRHPGSD
DAELRSLATE AAAGLIGEEP AYSRLAARLL TLAVREEAAG QGAHSFSASV ATGHREGLIA
DGTAAFVRTH AARLDALVAA AQADGADDRL GYFGLRTVHT RYLLRHPVTR RVIETPQHFL
LRVACGLAAD DGEEALTEVA ELYRLTSTLA YLPSSPTLFN SGTRHPQMSS CYLLDSPLDD
LDSVYERYGQ VARLSKHAGG IGLSYSRIRG RGSLIRGTNG LSNGIVPFLR TLDSSVAAVH
QGGRRKGAAC VYLETWHADL EEFLELRDST GEEARRTHHL NLAHWIPDEF MRRVEADAGW
SLFSPSDTPE LTDLWGDAFD AAYRRAEAAG LAVRTVPARE LYSRMMRTLA QTGNGWMTFK
DTSNRTANQT AEPGHVVHSS NLCTEILEVT DDGETAVCNL GSVNLAAHLH DDGTLDWERL
DATVRTAVTF LDRVVDVNYY PTPQAAASNS RWRPVGLGLM GLQDVFFRLR LPFDSPEARE
LSTRVSERIM LAAYEASAAL AERHGPLPAW ESTRTARGVL HPDHYPDAVP AWPERWSALR
ERVARTGLRN ALLLAIAPTA TIASIAGVYE CIEPQVSNLF KRETLSGEFL QVNAYLVAEL
KRLGRWDERT RDALRESSGS VQELDGIPDD VRALYRTAWE IPQRALIDMA AARTPYLDQS
QSLNLFLSSP TIGKLSSMYA YAWRSGIKTT YYLRSRPATR IARAAGGTAA NPTTAAPQDD
AAACSLENPE SCEACQ
//
