ID A0A0X3XJ84_9ACTN Unreviewed; 784 AA.
AC A0A0X3XJ84;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ADL34_29960 {ECO:0000313|EMBL:KUL69891.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL69891.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL69891.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL69891.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
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:KUL69891.1}.
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DR EMBL; LLZN01000091; KUL69891.1; -; Genomic_DNA.
DR RefSeq; WP_062668206.1; NZ_LLZN01000091.1.
DR AlphaFoldDB; A0A0X3XJ84; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000052945; 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:UP000052945}.
FT DOMAIN 586..608
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 86135 MW; B35AFA4BF0078848 CRC64;
MTIAPAEPAS AAAEPENDGP GAALLRTLTE LTADLPDADP GRVAAAALRG RSARADETEL
RELATEAAAG LISEDPAYSR LAARLLTLSI AAEAASQGVT TFTGSVATGH REGLVADRTA
AFVRTHAARL DALVDTGADD RFGYFGLRTL HSRYLLRHPH TRKVIETPQH FLLRVAAGLA
ADDTAGAVDE VAALYRLMSR LEYLPSSPTL FNSGTRHPQM SSCYLLDSPK DELDSIYDRY
HQVARLSKHA GGIGLSYSRV RARGSLIRGT NGHSNGIVPF LKTLDASVAA VNQGGRRKGA
AAVYLETWHS DIEEFLELRD NTGEDARRTH NLNLAHWVPD EFMRRVEADA PWSLFSPADV
PELVDLWGEE FDAAYREAER KGLARKTLPA RELYGRMMRT LAQTGNGWMT FKDAANRTAN
QTALPGHVVH SSNLCTEILE VTDDGETAVC NLGSVNLGAF VRGGDIDWER LDETVRTAVT
FLDRVVDINF YPTEQAGRSN ARWRPVGLGA MGLQDVFFQL RLPFDSPEAK ALSTRIAERI
MLAAYEASAD LAEREGPLPA WEKTRTARGV LHPDHYGVEL TWPERWAALR ERIDEVGLRN
ALLLAIAPTA TIASIAGVYE CIEPQVSNLF KRETLSGEFL QVNSYLVEEL KRLGVWDART
REALREANGS VQDFAWIPAD VRALYRTAWE IPQRGLIDMA AARTPFLDQS QSLNLFLETP
TIGKLSSMYA YAWKQGLKTT YYLRSRPATR IARAARATVP VPQVTDPDAV ACSLENPESC
EACQ
//
