ID A0A1X0UHR1_9NOCA Unreviewed; 721 AA.
AC A0A1X0UHR1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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 ORFNames=BJI47_20130 {ECO:0000313|EMBL:ORI18248.1};
OS Rhodococcus sp. 1168.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=2018041 {ECO:0000313|EMBL:ORI18248.1, ECO:0000313|Proteomes:UP000192546};
RN [1] {ECO:0000313|EMBL:ORI18248.1, ECO:0000313|Proteomes:UP000192546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1168 {ECO:0000313|EMBL:ORI18248.1,
RC ECO:0000313|Proteomes:UP000192546};
RA Nahar A.;
RT "Metabolic and lipid synthesis pathways analysis of sub-Antarctic
RT Rhodococcus luteus.";
RL Submitted (OCT-2016) 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:ORI18248.1}.
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DR EMBL; MKKY01000072; ORI18248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0UHR1; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000192546; 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:UP000192546}.
FT DOMAIN 573..595
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 721 AA; 81274 MW; 3B13955A2232C631 CRC64;
MAPTITDTAP AQTTVRADGD LDYHALNAML NLYGPNGEIQ FEKDREAANQ YFLQHVNQNT
VFFHDLDEKL DYLVEENYYE AEVLDQYSRE FVKFLINHAY SKKFRFPTFL GAFKYYTSYT
LKTFDGKRYL ERFEDRVCMV ALTLGAGDEA LATDLVDEII AGRFQPATPT FLNSGKKQRG
EPVSCFLLRI EDNMESIGRS INSALQLSKR GGGVALLLSN IREAGAPIKR IENQSSGVIP
IMKLLEDSFS YANQLGARQG AGAVYLHAHH PDVYKFLDTK RENADEKIRI KTLSLGIVIP
DITFELAKKN EDMYLFSPYD VERIYGVPFA DINVSETYYE MVDDKRIRKT KIKAREFFQT
LAELQFESGY PYIMFEDTVN RANPVKGKIT HSNLCSEILQ VSTPSTFNDD LSYSHVGKDI
SCNLGSLNIA KTMDSPDFGK TIAVAIRGLT AVSDQTHIFS VPSIEQGNND SHAIGLGQMN
LHGYLARERI HYGSTEGIDF TNIYFYTVVF HAIQASNQLS IARGEYFKGF PDSKYASGEF
FDKYTDEVWE PATSRVAALF ADAGVHIPTQ ADWSALKASV QEHGIYNQNL QAVPPTGSIS
YINNSTSSIH PVASKIEIRK EGKIGRVYYP APYLNNDNLE FYQDAYEIGY EKIIDTYAAA
TQHVDQGLSL TLFFKDTAST RDINRAQIYA WRKGIKTLYY IRLRQLALEG TEVEGCVSCM
L
//
