ID A0A3M8LAA0_9MICO Unreviewed; 701 AA.
AC A0A3M8LAA0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 Name=nrdE {ECO:0000313|EMBL:RNE62225.1};
GN ORFNames=EEJ31_08865 {ECO:0000313|EMBL:RNE62225.1};
OS Cryobacterium tepidiphilum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=2486026 {ECO:0000313|EMBL:RNE62225.1, ECO:0000313|Proteomes:UP000279859};
RN [1] {ECO:0000313|EMBL:RNE62225.1, ECO:0000313|Proteomes:UP000279859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-85 {ECO:0000313|EMBL:RNE62225.1,
RC ECO:0000313|Proteomes:UP000279859};
RA Wang Y.;
RT "Cryobacterium sp. nov., isolated from rhizosphere soil of lettuce.";
RL Submitted (NOV-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:RNE62225.1}.
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DR EMBL; RDSR01000013; RNE62225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8LAA0; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000279859; 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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 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 Pfam; PF08343; RNR_N; 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:UP000279859}.
FT DOMAIN 553..575
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 701 AA; 79247 MW; 57AEE2750E26938F CRC64;
MDYHSLNAML NLYGANGEIQ FDKDREAARE YFLQHVNQNT VFFHSLKERL DYLVEKQYYE
KAVLDKYSFE FITTLNDLAY SKKFRFQTFL GAFKYYTSYT LKTFDGKRYL ERFEDRVVMT
ALGLADGDEA LAISLVEEII AGRFQPATPT FLNTGKAQRG ELVSCFLLRI EDNMESISRG
INSSLQLSKR GGGVALLLSN IREAGAPIKQ IENQSSGIIP VMKLLEDSFS YANQLGARQG
AGAVYLHAHH PDIMRFLDTK RENADEKIRI KTLSLGVVVP DITFELAKKD EDMYLFSPYD
VERVYGVPFA DISVSEKYQE MVDDPRIKKS KMKAREFFQT IAEIQFESGY PYIMFEDTVN
RANPIQGRIN MSNLCSEILQ VNTPTTYNED LSYDTIGKDI SCNLGSMNIA LAMDSPDFGL
TVETAIRGLN AVSEQSHISS VRSIEDGNDK SHAIGLGQMN LHGYLARERV FYGSDEGIDF
TNIYFYTVLF HALRASNKLA IERGHAFDGF ENSTYASGTF FDKYTDQVWQ PTTERGAELF
AKSAVAIPTQ ADWAELKASV MKHGIYNQNL QAVPPTGSIS YINNSTASIH PIASKIEIRK
EGKLGRVYFP APFMTNDNLE FYQDAYEIGA EKIIDTYAAA TQHVDQGLSL TLFFKDTATT
RDINKAQIYA WRKGIKTIYY IRLRQMALEG TELEMCVSCA L
//
