ID   A0A223S0A3_9ACTN        Unreviewed;       849 AA.
AC   A0A223S0A3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-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=CDO52_01025 {ECO:0000313|EMBL:ASU81562.1};
OS   Nocardiopsis gilva YIM 90087.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1235441 {ECO:0000313|EMBL:ASU81562.1, ECO:0000313|Proteomes:UP000215005};
RN   [1] {ECO:0000313|EMBL:ASU81562.1, ECO:0000313|Proteomes:UP000215005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90087 {ECO:0000313|EMBL:ASU81562.1,
RC   ECO:0000313|Proteomes:UP000215005};
RA   Yin M., Tang S.;
RT   "The complete genome sequence of Nocardiopsis gilva YIM 90087.";
RL   Submitted (AUG-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; CP022753; ASU81562.1; -; Genomic_DNA.
DR   RefSeq; WP_017619563.1; NZ_CP022753.1.
DR   AlphaFoldDB; A0A223S0A3; -.
DR   KEGG; ngv:CDO52_01025; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000215005; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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; PS51161; ATP_CONE; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215005}.
FT   DOMAIN          5..97
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   REGION          787..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  93396 MW;  F7C9F2250FA197F2 CRC64;
     MTLDLDVAAA EPAHANPASD PMERVGQVVH EACAGLTGVS ADKVIAETRR GLYPGITSDE
     LELALVMAAR TFVEADPDYS HVAARLLLDK LRREALTFLS GAFDEADQAQ MAERYSDYLA
     AYIARGVELG QLDPRLATFD LTRLGAALRP ERDLDFTFLG LQTLYDRYFL HSDGTRYELP
     QAFFMRVAMG LALNEDDREA RAIEFYGLIS SFDFMCSTPT LFNAGTQRAQ LSSCFLTTIG
     DDLQSIFHGI SNNALLSKYS GGLGNDWTPV RGIGAHIKGT NGQSQGVVPF LKIANDTAVA
     VNQGGKRKGA VCAYLETWHI DIEEFLDLRK NTGDDRRRTH DMNTANWVPD LFLQRVEANG
     EWTLFSPDEV PDLHDLYGAE FAEAYTAYER AAEAGEIKVW RRVRAVDLWR RMLTMLFETG
     HPWIAFKDPC NLRSPQQHSG VVHSSNLCTE ITLNTSADEV AVCNLGSVNL ARHVTEDGID
     AERLRRTVHT AVRMLDNVID VNFYTIPEAE RANMRHRPVG LGLMGFQDAL FRLRLPMGSQ
     GAVEFADESM ELISYHAITA SMELAAERGA YETFEGSLWS KGVLPIDSLQ LLDDARGGDL
     DVDTTARLDW ETLRERVRTV GMRNSNVMAI APTATIANIT GVGQSIEPIY RNLFVKSNMS
     GDFTVVNPYL VRDLKERGLW DDDMVSQLKL YDGSLGAIDR VPDDLKDLYA TAFEVDPSWL
     VDAGSRRQKW LDQAQSLNLY MAAPSGRKLD ELYRRAWRKG LKTTYYLRSQ SATHVEKSTL
     KGTDGKLNAV AATPTPTAAP SPSPAAAVSP GASAPAPTSA AGTPSTAPEL DPDAGSTCSI
     DDPDCEACQ
//