ID A0A1W7CV53_9ACTN Unreviewed; 821 AA.
AC A0A1W7CV53;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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=CAG99_06895 {ECO:0000313|EMBL:ARQ68617.1};
OS Streptomyces marincola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ68617.1, ECO:0000313|Proteomes:UP000194218};
RN [1] {ECO:0000313|EMBL:ARQ68617.1, ECO:0000313|Proteomes:UP000194218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ68617.1,
RC ECO:0000313|Proteomes:UP000194218};
RA Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL Submitted (MAY-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}.
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DR EMBL; CP021121; ARQ68617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7CV53; -.
DR KEGG; smao:CAG99_06895; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000194218; 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:UP000194218}.
FT DOMAIN 613..635
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 821 AA; 89845 MW; BA7E23FC216A766C CRC64;
MPLPYHTHAS TRPPARPAPW PPRFEGEHRV TTAPVAPAEP VTAALPRLLT DLTADLPAAD
PDRVATAVLR GRHAGSDEAE LRSLAIEAAA GLIAEDPAYS RLAARLLTLA IRDEAAGQGA
VSFSASVATG HREGLIGDGT AAFVRRHADR LDALAETAVA EGADDRFEYF GLRTVESRYL
LRHPLTRRVI ETPQHFLLRV ACGLADGDSE QALAEVAELY RLTSSLAYLP SSPTLFNSGT
RHPQMSSCYL LDSPKDELDS IYERYHQVAR LSKHAGGIGL SYTRVRARGS LIRGTNGKSN
GIVPFLRTLD ASVAAVNQGG RRKGAACVYL ETWHADIEEF LELRDNTGED ARRTHNLNLA
HWIPDEFMRR VEADAEWSLF SPADVPELTD LWGEEFDAAY RRAEAEGLAV RALPARQLYA
RMMRTLAQTG NGWMTFKDAA NRTANQTAEP GAVVHSSNLC TEILEVTDDG QTAVCNLGSV
NLAAHLGPDG TPDWERLDAT VRTAVTFLDR VVDINFYPTS QAGSSNTRWR PVGLGVMGLQ
DVFFRLRLPF DSPEARELST RIAERIMLTA YETSADLAER HGPHPAWDAT RTARGVLHPD
HYPDAEPAWR SRWEALRERI ARTGMRNSLL LAIAPTATIA SIAGVYECIE PQVSNLFKRE
TLSGEFLQVN TYLVNDLKRL GLWNDATREA LREANGSVEG VAGLPEEIRA LYRTAWELPQ
RALIDMAAAR TPYLDQSQSL NLFLAAPTIG KLSSMYAYAW KRGLKTTYYL RSRPATRIAQ
AARAGTATAV PAPGPAAAVP VVPEQAVACS LENPESCEAC Q
//