ID A0A344TW78_9ACTN Unreviewed; 800 AA.
AC A0A344TW78;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C0216_05035 {ECO:0000313|EMBL:AXE22899.1};
OS Streptomyces globosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE22899.1, ECO:0000313|Proteomes:UP000252004};
RN [1] {ECO:0000313|EMBL:AXE22899.1, ECO:0000313|Proteomes:UP000252004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZH-48 {ECO:0000313|EMBL:AXE22899.1,
RC ECO:0000313|Proteomes:UP000252004};
RA Ran K., Li Z., Wei S., Dong R.;
RT "Draft genome Sequence of streptomyces globosus LZH-48.";
RL Submitted (JAN-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; CP030862; AXE22899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344TW78; -.
DR KEGG; sgz:C0216_05035; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000252004; 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:UP000252004}.
FT DOMAIN 596..618
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 87178 MW; 31965DAE514D6D7B CRC64;
MTIAPSAPRA ESDPSDHGAE AGGPGAALLR TLTELTADLP DTDPGRVAAA ALRGRSAAAD
EAELRGLATE AAAGLISEDP AYSRLAARLL TVAVAEEAAS QGSTSFSASV EVGHREGLIA
DRTAEFVRLH ASRLDALVEH TLAEGADDRF GFFGLRTLHS RYLLRHPITR QVIETPQHFM
LRVACGLAAD DSAAAVEEVA SLYRLMSRLD YLPSSPTLFN SGTRHPQMSS CYLLDSPLDE
LDSIYDRYHQ VARLSKHAGG IGLSYSRIRA RGSLIRGTNG HSNGIVPFLK TLDASVAAVN
QGGRRKGAAA VYLETWHADI EEFLELRDNT GEDARRTHNL NLAHWIPDEF MRRVNADGEW
SLFSPSDVPE LVDLYGEEFD AAYTKAEQAG LAKKTMPARE LYGRMMRTLA QTGQGWMTFK
DASNRTANQT ALPGTVVHSS NLCTEIIEVT NDGETAVCNL GSVNLGAFVL AETGEMDWER
LDETVRTAVT FLDRVVDINF YPTEQAGRSN AKWRPVGLGA MGLQDVFFKL RLPFDSAEAK
ALSTKIAERI MLAAYEASAD LAEKHGPVPA WAETRTAQGV LHPDHYGTER AWPERWEALR
TRIAETGMRN SLLLAIAPTA TIASIAGVYE CIEPQVSNLF KRETLSGEFL QVNAYLVEDL
KKLGVWDAQT REALRDSSGS VQGFNWIPAD VRELYRTAWE IPQRGLIDMA AARTPYLDQS
QSLNLFMETP TIGKLSSMYA YAWKQGLKTT YYLRSRPATK IARAASGAAV PAAATPLPQA
VDADALACSL ENPESCEACQ
//
