ID A0A0X3S9G7_9ACTN Unreviewed; 794 AA.
AC A0A0X3S9G7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=ADL25_18195 {ECO:0000313|EMBL:KUJ40490.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ40490.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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:KUJ40490.1}.
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DR EMBL; LMWH01000172; KUJ40490.1; -; Genomic_DNA.
DR RefSeq; WP_059128809.1; NZ_LMWH01000172.1.
DR AlphaFoldDB; A0A0X3S9G7; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054048; 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:UP000054048}.
FT DOMAIN 594..616
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 794 AA; 87267 MW; B7DE722471AD0324 CRC64;
MTIAPADPAS ATPSTPPVVT DGPGAALLRT LTELTADLPD ADPGRVAAAA LRGRSARKDA
EIVAELRELA TEAAAGLISE DPAYSRLAAR LLTIGIRAEA ASQGVTSFTE SIAVGHREGL
VADRTAEFVL LHAERLDALV DQGADDRFGY FGLRTLHSRY LLRHPITRKV VETPQHFMLR
VASGLAEDAT TRSVDEVAAL YGLMSRLDYL PSSPTLFNSG TRHPQMSSCY LLDSPKDELD
SLYDRYHQVA RLSKHAGGIG LSYSRIRSRG SLIRGTNGHS NGIVPFLKTL DASVAAVNQG
GRRKGAAAVY LETWHSDIEE FLELRDNTGE DARRTHNLNL AHWVPDEFMR RVDADGQWSL
FSPSDVPELV DLWGTEFDAA YRRAEAAGLA KKTMPARDLY GRMMRTLAQT GNGWMTFKDA
ANRTANQTAE PGHVIHSSNL CTEILEVTDD GETAVCNLGS VNLGAFVDRA NGDLDWERLD
ATVRTAVTFL DRVVDINFYP TEQAGRSNAK WRPVGLGVMG LQDVFFQLRL PFDSPEAKTL
STRIAERIML AAYEASADLA ERNGPLPAWE KTRTARGVLH PDHFGVEPTW PERWAALRER
IAAVGMRNSL LLAVAPTATI ASIAGVYECI EPQVSNLFKR ETLSGEFLQV NSYLVRDLKE
LGVWDARTRE ALRDSNGSVQ DFAWIPEDVR GLYRTAWEIP QRGLIDMAAA RTPFLDQAQS
LNLFMETPTI GKLSSMYAYA WKQGLKTTYY LRSRPATRIA RAAQARPTIP VQQVADLDAV
ACSLENPESC EACQ
//
