ID A0A2A9G1I9_9PSEU Unreviewed; 1019 AA.
AC A0A2A9G1I9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=ATK36_0242 {ECO:0000313|EMBL:PFG56722.1};
OS Amycolatopsis sulphurea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=76022 {ECO:0000313|EMBL:PFG56722.1, ECO:0000313|Proteomes:UP000243542};
RN [1] {ECO:0000313|EMBL:PFG56722.1, ECO:0000313|Proteomes:UP000243542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46092 {ECO:0000313|EMBL:PFG56722.1,
RC ECO:0000313|Proteomes:UP000243542};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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:PFG56722.1}.
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DR EMBL; PDJK01000001; PFG56722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9G1I9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000243542; 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; 2.
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:UP000243542}.
FT DOMAIN 20..120
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 132..221
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 926..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..981
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 111228 MW; F96D69AE86CC1A42 CRC64;
MSVETGTRPP ATADQAPNTV HVIRRDGSVS PFDAGKISVA LTKAFLAVEG GDAAASSRVH
HVVAELTGQV EAGLLRHAGP ETALHIEQIQ DQVELALMRG EHHKVARAYV LYREERTKAR
AAAAPAPAEA AITVKGADGT VRPLDWARVA HVVGEAVAGL EDVSAEPVLA EAKRNLYDGI
STDELALAQI MAARVLVEQE PNYSYVSARL LLDKLRGEAL GYLAGAPRLA SQDEMAREYP
AYFRAYLRRA VELELVDGEL LGFDLDRITA ALHAERDLDF GFLGLQTLYD RYFQHHNGVR
FELPQAFFMR VAMGLAIRED DREARAIEFY ELLSTFHFMA STPTLFNSGT TRAQLSSCFL
TTVDDDLDSI FQAYKNNALL AKYSGGLGND WTPVRGLGAH IKGTNGQSQG VVPFLKIAND
TAVAVNQGGK RKGAACAYLE TWHVDIEEFL DLRKNTGDDR RRTHDMNTAN WVPDEFLRRV
EADAQWTLFS PNETPDLHDL FGTAFAERYR EYEAAAERGE IKVFRRVRAV ELWRRMLTML
FETGHPWITF KDPCNLRSPQ QHIGVVHSSN LCTEITLNTN SEEVAVCNLG SVNLLKHVTP
SGVDTARLEQ TVRTAVRMLD NVIDINFYTI PEARRSNLRH RPIGLGLMGF QDALFEIGVP
LSSDAAVRFA DESMEHLSYY AISASTDLAQ ERGRYQSFEG SLWSRGILPI DSLQLLIDAR
QGDALDVDTS STLDWAPLRE RVKTVGMRNS NVMAIAPTAT ISNICGVGQS IEPLFQNLYV
KSNMSGDFTV VNPHLVRSLK ARGLWDEVMV SDLKYFDGSL GQIDRVPDDL KALYATAFEI
ESKWLVDAGS RRQKWIDQAQ SLNLYIDAPS GRKLDELYRY AWHKGLKTTY YLRARSATHV
EKSTLRGTDG KLNAVSATPA AAAPAASPAA APSAGPAPSA GLAPSAGPAP ASSPSAAPAP
APSPSPSPAP SPSPAAAVPA TPPAAQPESK ELPKVDDVDF VATEGAACRI DDPDCEACQ
//
