ID A0A243S7Y4_9ACTN Unreviewed; 799 AA.
AC A0A243S7Y4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=CA983_07985 {ECO:0000313|EMBL:OUD03736.1};
OS Streptomyces swartbergensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=487165 {ECO:0000313|EMBL:OUD03736.1, ECO:0000313|Proteomes:UP000195105};
RN [1] {ECO:0000313|EMBL:OUD03736.1, ECO:0000313|Proteomes:UP000195105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC13 {ECO:0000313|EMBL:OUD03736.1};
RA Le Roes-Hill M., Prins A., Durrell K.A.;
RT "Biotechnological potential of actinobacteria isolated from South African
RT environments.";
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}.
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:OUD03736.1}.
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DR EMBL; NGFN01000031; OUD03736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243S7Y4; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000195105; 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}.
FT DOMAIN 601..623
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 553..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 87761 MW; A8523A30D6721093 CRC64;
MTIAPADPVS AAEEEHDGPG AALLRTLTEL TADLPDADPG RVAAAALRGR SARADESELR
ELATEAAAGL ISEDPAYSRL AARLLTIGIR AEAASQGVTC FTESVAVGHR EGLIADRTAE
FVRVHAARLD ALIDTAADDR FGYFGLRTLH SRYLLRHPIT RKVIETPQHF MLRVAAGLAE
DDTTRALDEV AALYRLMSRL DYLPSSPTLF NSGTRHPQMS SCYLLDSPKD ELDSIYDRYH
QVARLSKHAG GIGIAYSRIR ARGSLIRGTN GHSNGIVPFL KTLDTSVAAV NQGGRRKGAA
AVYLETWHSD IEEFLELRDN TGEDARRTHN LNLAHWVPDE FMRRVNADAH WSLFSPSDVP
ELVDLWGEEF DAAYRAAEAK GLAKKTLPAR ELYGRMMRTL AQTGNGWMTF KDAANRTANQ
TAEPGHVVHS SNLCTEILEV TSDGETAVCN LGSVNLGAFV DQTGGDIDWE RLDETVRTAV
TFLDRVVDIN FYPTEQAGRS NARWRPVGLG VMGLQDVFFK LRLPFDSPEA KALSTRIAER
IMLAAYEASA ELAERPQAPT TSSGAGGTPI GPLPAWEKTR TARGVLHPDH YDVEPTWPER
WAALRERIAA TGMRNSLLLA IAPTATIASI AGVYECIEPQ VSNLFKRETL SGEFLQVNSY
LVEELKRLGV WDARSREALR EANGSVQDFA WIPDDVRALY RTAWEIPQRG LIDMAAARTP
FLDQSQSLNL FLETPTIGKL SSMYAYAWKS GLKTTYYLRS RPATRIARAA QATVPVQATP
DPEATACSLE NPESCEACQ
//
