ID   S5XQH6_PARAH            Unreviewed;       708 AA.
AC   S5XQH6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=JCM7686_0201 {ECO:0000313|EMBL:AGT07312.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT07312.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT07312.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT07312.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(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}.
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DR   EMBL; CP006650; AGT07312.1; -; Genomic_DNA.
DR   RefSeq; WP_020948952.1; NC_022041.1.
DR   AlphaFoldDB; S5XQH6; -.
DR   STRING; 1367847.JCM7686_0201; -.
DR   KEGG; pami:JCM7686_0201; -.
DR   PATRIC; fig|1367847.3.peg.143; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_4_1_5; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000015480; Chromosome.
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:UP000015480}.
FT   DOMAIN          560..582
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   708 AA;  79957 MW;  F60DBA6E43F7D96D CRC64;
     MLDNGVKAEL DYHALNAMLN LYDNEGNIRF DADRKAAHQY FLQHVNQNTV FFHSLDEKLD
     YLVEEGYYEA EVLDQYSKNF MRQIWDEAYR KKFRFPTFLG AFKYYTSYTL KTRDGQRYLE
     RYEDRVVMVS LALARGDEKL ATRFMDEILS GRFQPATPTF LNAGKKSRGE LISCFLLRIE
     DNMESIGRSI NSSLQLSKRG GGVALMLTNI RESGAPIKGI ENQSSGVIPV MKLLEDSFSY
     ANQLGARQGA GAVYLNAHHP DILRFLDTKR ENADEKIRIK TLSLGVVIPD VTFDLAKKNE
     DMYLFSPHDV QKVYGVPFSE ISVTEKYQEM VDDKRIKKKK INARAFFQTL AEIQFESGYP
     YIMFEDTVNK ANPIDGRITM SNLCSEILQV NEASEFSEDL SYSKMGTDIS CNLGSLNIAA
     TMDGPDFGAT VEAAIRALTA VSEMSAIESV PSIRRGNDEA HAVGLGQMNL HGFLARERIH
     YGSPEGVEFT SVYFAAIAYH AIRASNLIAR EKGETFKGFE KSKYADGSFF AKYTEQDWLP
     VSEEVVRVFD GIELPTREDW AALKADVMAH GLYNRNLQAV PPTGSISYIN NSTSSIHPIV
     AKIEIRKEGK IGRVYYPAAF MNNENLEYYR DAYEIGPEKI IDTYAAATEH VDQGLSLTLF
     FPAEATTRDI NKAQIYAWKK GIKTIYYIRL RQTALEGTEI QGCVSCSL
//