ID A0A101NIU8_9ACTN Unreviewed; 787 AA.
AC A0A101NIU8;
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=AQI88_23680 {ECO:0000313|EMBL:KUM93990.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM93990.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM93990.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM93990.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
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:KUM93990.1}.
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DR EMBL; LMWL01000042; KUM93990.1; -; Genomic_DNA.
DR RefSeq; WP_067002799.1; NZ_KQ948027.1.
DR AlphaFoldDB; A0A101NIU8; -.
DR STRING; 67285.AQI88_23680; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054241; 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:UP000054241}.
FT DOMAIN 585..607
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 787 AA; 86715 MW; 9C73EC910E6D3CD8 CRC64;
MTIAPADPAS VSDLETDGPG TALLRTLTEL TADLPDADPG RVAAAALRGR SARADEAELR
ELATEAAAGL ISEDPAYSRL AARLLTLTIR AEAASQGVTS FTESVAVGHR EGLVADRTAE
FVRLHAGRLD SLIDPLADDR FGYFGLRTLH SRYLLRHPIT RQVIETPQHF MLRVAAGLAE
DDSTRALDEV AALYGLMSRL DYLPSSPTLF NSGTRHPQMS SCYLLDSPLD ELDSIYDRYH
QVARLSKHAG GIGLSYSRIR SRGSLIRGTN GHSNGIVPFL KTLDASVAAV NQGGRRKGAA
AVYLETWHSD IEEFLELRDN TGEDARRTHN LNLAHWIPDE FMRRVNADGQ WSLFSPADVP
ELVDLWGEEF DAAYRRAEEQ GLAKKTIPAR DLYGRMMRTL AQTGNGWMTF KDAANRTANQ
TAVPGHVVHS SNLCTEILEV TDDGETAVCN LGSVNLGAFV SDGEIDWKRL DETVRTAVTF
LDRVVDINFY PTEQAGRSNA KWRPVGLGAM GLQDVFFKLR LPFDSPEARA LSTRIAERIM
LAAYEASADL AERSGPLPAW EKTRTAQGVL HPDHYDVELN WPERWAALRE RIAAVGMRNS
LLLAIAPTAT IASIAGVYEC IEPQVSNLFK RETLSGEFLQ VNSYLVKDLK ELGVWDARTR
EALRESNGSV QDFVWIPADV RALYRTAWEI PQRGLIDMAA ARTPFLDQAQ SLNLFLETPT
IGKLSSMYAY AWKSGLKTTY YLRSRPATRI ARAAQAQTQA TIPVQQVADP DAVACSLENP
ESCEACQ
//
