ID A0A2S6H1P3_9PSEU Unreviewed; 787 AA.
AC A0A2S6H1P3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CLV40_101527 {ECO:0000313|EMBL:PPK71337.1};
OS Actinokineospora auranticolor.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155976 {ECO:0000313|EMBL:PPK71337.1, ECO:0000313|Proteomes:UP000239203};
RN [1] {ECO:0000313|EMBL:PPK71337.1, ECO:0000313|Proteomes:UP000239203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YU 961-1 {ECO:0000313|EMBL:PPK71337.1,
RC ECO:0000313|Proteomes:UP000239203};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-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}.
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:PPK71337.1}.
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DR EMBL; PTIX01000001; PPK71337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6H1P3; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000239203; Unassembled WGS sequence.
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; PF03477; ATP-cone; 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:UP000239203}.
FT DOMAIN 11..100
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 787 AA; 86616 MW; 3BAEDE0AE9BAD50C CRC64;
MTVVDSVVTT MRVRKRDGAL EPVDVNRIVR AVARRAVGLT EVDPLRVATK TISGLYDGAT
TEELDKLSIQ TAAALVAEEP EYSRLAAGLL SAFIDKEVRR HGVGSFSESI ALGHAEGLIG
DTTAAFVAAN AIDLDDAIDL DADRRFEYFG LRTVYDRYLL RHPARRTVIE APQYWLLRVA
CGLSRTAAEA VGFYRLMSSL AYLPSSPTLF NSGTVHTQMS SCYLLDSPRD ELESIYERYA
QIARLSKFAG GIGVQWSRVR SRGALIRGTN GHSNGIVPWL RTLDASVAAV NQGGRRKGAA
CVYLETWHPD VEEFLELRDN TGEDARRTHN LNLANWIPDE FMRRVEADSD WSLFDPDEVP
GLVDLWGDDF DRAYRAAEEA GRAVRTVRAR DLYGRMIRTL AQTGNGWMTF KDTANRTCNQ
TAEPGNVVHL SNLCTEILEV TSDDETAVCN LGSVNLGAHV LVDGAGGDAS GGIDWERLRA
TVRTAVVFLD RVIDINYYPT AQAAASNPRW RPVGLGVMGL QDVFFKLRLP FDSPAARELS
TRIAEEIYLT ALESSAELAA SAGAHPAYAR TRAARGDLQP DLWGVTPTQT ERWARVRARI
AEHGLRNSLL VAIAPTATIA SIAGCFECVE PQVSNTFKRE TLSGEFLQIN SYLVRELKAR
GLWTDEIRSR LKRDDGSAQG VTELPADVRE LYRTAWELPQ KALIELAAAR GPYVDQSQSL
NLFVAAPTIG KLSSMYLYAW KAGLKTTYYL RSRPATRIQQ ATVAVPEATV DAIACSLENP
ESCEACQ
//
