ID A0A2W0CZ36_9MICO Unreviewed; 701 AA.
AC A0A2W0CZ36;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=DEI89_11330 {ECO:0000313|EMBL:PYY32971.1};
OS Curtobacterium sp. MCBD17_030.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2175649 {ECO:0000313|EMBL:PYY32971.1, ECO:0000313|Proteomes:UP000248059};
RN [1] {ECO:0000313|EMBL:PYY32971.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBD17_030 {ECO:0000313|EMBL:PYY32971.1};
RA Chase A.B., Gomez-Lunar Z., Lopez A.E., Li J., Allison S.D., Martiny A.C.,
RA Martiny J.B.H.;
RT "Emergence of Soil Bacterial Ecotypes Along a Climate Gradient.";
RL Submitted (JUN-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:PYY32971.1}.
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DR EMBL; QKLI01000012; PYY32971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W0CZ36; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000248059; 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}.
FT DOMAIN 553..575
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 701 AA; 79378 MW; 9EDBE68D03EC317D CRC64;
MDYHSLNAML NLYDADGNIQ FDKDREAAKQ FFLQHVNQNT VFFHNLKERL DYLVENEYYE
QATIDLYSMD FIQRLNDLAY SKKFRFQTFL GAFKYYTSYT LKTFDGKRYL ERFEDRVVMT
ALGLAQGNEQ LAIDLVEEII AGRFQPATPT FLNTAKAQRG ELVSCFLLRI EDNMESISRG
INSSLQLSKR GGGVALLLSN IREAGAPIKQ IENQSSGIIP VMKLLEDSFS YANQLGARQG
AGAVYLSAHH PDIMKFLDTK RENADEKIRI KTLSLGVVVP DITFELAKNN EDMYLFSPYD
VEKVYGVPFG DVPISENYRA MVDDSRIKKT KIKARDFFTT IAEIQFESGY PYIVFEDTVN
KANPIKGRIN MSNLCSEILQ VNTPTTFNED LSYKEIGKDI SCNLGSLNIA LTMDSPDFGK
TIETAIRGLT SVSQMSHISS VRSVEDGNDK SHAIGLGQMN LHGYLARERV YYGSEEGIDF
TNIYFYTVLF HALRASNNIA IETGETFDGF RDSKYASGEF FDKYTDQVWT PATPRVASLF
DNANITIPTQ DDWKALKASI QQYGIYNQNL QAVPPTGSIS YINHSTSSIH PIASKIEIRK
EGKLGRVYYP APFMTNDNLD YYQDAYEIGP EKIIDTYAAA TQHVDQGLSL TLFFKDTATT
RDINKAQIYA WRKGIKTIYY IRLRQLALEG TEVEGCVSCM L
//
