ID A0A024H1K3_9MICC Unreviewed; 691 AA.
AC A0A024H1K3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=nrdE1 {ECO:0000313|EMBL:CCQ45883.1};
GN ORFNames=ARTSIC4J27_1843 {ECO:0000313|EMBL:CCQ45883.1};
OS Pseudarthrobacter siccitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ45883.1, ECO:0000313|Proteomes:UP000035722};
RN [1] {ECO:0000313|Proteomes:UP000035722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT Producing Desiccation-Tolerant Microorganism.";
RL Genome Announc. Announc.2:e00526-e00514(2014).
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:CCQ45883.1}.
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DR EMBL; CAQI01000041; CCQ45883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024H1K3; -.
DR STRING; 861266.ARTSIC4J27_1843; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000035722; 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 543..565
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 691 AA; 78857 MW; 3699D2B1FCAA954B CRC64;
MLNLYGPSGE IQFEADREAA HQYFLQHVNN NTVFFHDLEE KLEYLVKNDY YERETLDQYT
MNFIRDLFNR AYKKKFRFET FLGAFKFYTS YTLKTFDGKR FLERYEDRVC MVALHLARGN
EQLALQMVDE IIEGRFQPAT PTFLNAGKKQ RGELVSCFLL RIEDNMESIG RSINSALQLS
KRGGGVAFAL TNIREVGAPI KQIENQSSGV IPVMKLLEDS FSYANQLGAR QGAGAVYLHA
HHPDIYRFLD TKRENADEKI RIKTLSLGVV IPDITFELAK KDEDMYLFSP YDVERVYGMP
FSDVSVTEKY YEMVDDSRIK KTKIKAREFF QTLAEIQFES GYPYIMFEDK VNRANPIDGK
IIMSNLCSEI LQVSQPTTYN DDLSYADTGK DISCNLGSLN IAKTMDSPDF GLTIETAIRS
LSAVSDMSNI TSVPSIAKGN DQSHAIGLGQ MNLHGYLARE RVHYGSEEGL DFTNIYFYSV
VYHAIRASNL LSIETGQTFG GFEKSKYASG EFFDKYTEQE WMPQTEKVRE LFKNVHIPTQ
ADWLALKASV MEHGIYNQNL QAVPPTGSIS YINNSTSSIH PVASKIEIRK EGKIGRVYYP
APYLTNDNLE YYQDAYEIGY EKVIDTYAAA TQHVDQGLSL TLFFKDTATT RDINKAQIYA
WKKGIKTIYY IRLRQLALEG TEVEGCVSCM L
//
