ID W9G5S4_9MICO Unreviewed; 870 AA.
AC W9G5S4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=N865_14140 {ECO:0000313|EMBL:EWT00662.1};
OS Intrasporangium oryzae NRRL B-24470.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT00662.1, ECO:0000313|Proteomes:UP000019489};
RN [1] {ECO:0000313|EMBL:EWT00662.1, ECO:0000313|Proteomes:UP000019489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT00662.1,
RC ECO:0000313|Proteomes:UP000019489};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) 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:EWT00662.1}.
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DR EMBL; AWSA01000037; EWT00662.1; -; Genomic_DNA.
DR AlphaFoldDB; W9G5S4; -.
DR STRING; 1386089.N865_14140; -.
DR PATRIC; fig|1386089.3.peg.3107; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000019489; 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:UP000019489}.
FT DOMAIN 27..118
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 96137 MW; 911845BA4DA13413 CRC64;
MNTPLQDPTH HETAGPSRPV PTPGTHVRVT KRDGTREPFD ADRINRAVER ATEGLDNAVG
LTVQIASELA ITLFDGITTE ELDQAAIQVA VQNVKDDPDF DRVAARLLRT TMYKRVLGGY
ESGLELTLLH RARFPGHVRY AVEHGLLDAR LGSAFDLERL ADELDPEHDE LLTYIGVVTM
RNRYLLAGPD GTDVEVPQYF WMRVAMGLSL NEEDATGAAI RFYRAMSRLE YLPAGSTLVN
AGTPQPQLSN CFVLQMEDDI EHIAKSVRDV MWITKGTGGI GLSVTKLRAE GSPIRSNNTT
STGPIPFMHT IDSTLRAVSR GGKKFGALCF YMENWHLDFP QFLDLRQQAG DPYRRTRTAN
TAVWISDEFM RRVERDETWY LFDPLETPDL VELTGAAFSR RYADYVDLAE QGRLRAFRTV
RAREQFTAIL VALQTASHPW LTWKDTVNLR ALNDNTGTIH LSNLCTEITL PQDRDNSAVC
NLASVNLARH LRTDLTTGLP QGSDGPTGLE AAVDWERLEA TVRTAVRQLD NLIDITLSSV
PESERSNEAN RAVGLGMMGL TDVIERLGLI YGSDASLELV DRVTEFISFH AIDASADLAR
TRGSYPRFAG SGWSRGRVPL DTLADLEADR GVPVDVDRSA RLDWDVLRNK VAGGMRNATL
MAVAPTASIG LVAGTTPGLD PQFSQLFSRT TSSGKFLEVN RNLVAALKQR GLWELTREDL
LRSQGDVQGI DAIPAELREV YRTSFQLSPY AFLHVAARAQ KWVDQAISRT MYLETRDLGE
MARIYGAAWR MGVKTTYYLH VKPRHTAEQS TVRVNKAATT GRATGGFGFA RPAAPGAVSA
TSPDETERAS IGGLVCPTDP QERLECDACQ
//
