ID   Q0PCA1_CAMJE            Unreviewed;       789 AA.
AC   Q0PCA1;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 110.
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=nrdA {ECO:0000313|EMBL:CAL34205.1};
GN   OrderedLocusNames=Cj0024 {ECO:0000313|EMBL:CAL34205.1};
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34205.1, ECO:0000313|Proteomes:UP000000799};
RN   [1] {ECO:0000313|EMBL:CAL34205.1, ECO:0000313|Proteomes:UP000000799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA   Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA   Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA   Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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=a 2'-deoxyribonucleoside 5'-diphosphate + [thioredoxin]-
CC         disulfide + H2O = a ribonucleoside 5'-diphosphate + [thioredoxin]-
CC         dithiol; 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:ARBA00047754,
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL111168; CAL34205.1; -; Genomic_DNA.
DR   PIR; C81418; C81418.
DR   RefSeq; WP_002865087.1; NC_002163.1.
DR   RefSeq; YP_002343496.1; NC_002163.1.
DR   AlphaFoldDB; Q0PCA1; -.
DR   STRING; 192222.Cj0024; -.
DR   PaxDb; 192222-Cj0024; -.
DR   EnsemblBacteria; CAL34205; CAL34205; Cj0024.
DR   GeneID; 904363; -.
DR   KEGG; cje:Cj0024; -.
DR   PATRIC; fig|192222.6.peg.24; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_3_0_7; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:InterPro.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   NCBIfam; NF006279; PRK08447.1; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 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; PS51161; ATP_CONE; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000799}.
FT   DOMAIN          1..91
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   789 AA;  90052 MW;  B52387A96B098B0B CRC64;
     MKVIKRNGRT EELDVSKIKK CTSDAVKDLE GVNLSELELD AKIQFRDGIS TEEIQKTLIK
     TAVDKIDIDC PNWTFVAARL FLFDLYKKVN GMNRYNHLRE YFQKGEKEGR ILLGLKEKYD
     LDDLNAYIKP ERDMQFTYLG IKTLYDRYLI KDSKGMPIEL PQQMFMAIAM FLAQNEFNPQ
     EWAKKFYDLI SKFELMLATP TLSNARTTRH QLSSCYIGST PDNIEGIFDS YQEMALLSKF
     GGGIGWDWSK VRAMGGSIDG HKNAAGGIIP FLKITNDIAV AVDQLGTRKG AIAVYIEPWH
     MDISDFIDLR KNSGEERRRA HELFPALWIN DLFMKRVRAN DKWTLFDPAD TADLCDLYGE
     AFEKRYEEYE KDESITKEIV EAKELWKKIL LNYFETGLPF LCFKDSANRA NPNAHVGIIR
     SSNLCTEIFQ NTEPNYYQIK VVFENGDELH FDEEQKVVID GGYEKPAKKI STLDSIEGNK
     VYIVEKYKND GKTAVCNLAS INLSKVYTKE DIERVVPTAI RMLDNVIDLN FYPHRKVKDT
     NLKSRAIGLG VMGEAQMLAE AKIHWGSDEH LNKIDEIMEQ ISFEAINASS NLALEKGSYE
     DFEGSNWSKG IFPIDVASPK AKALTLREGL FDQSECDWVK LREKVKKDGM RNGYLMAIAP
     TSSISILVGT TQTIEPVYKR KWFEQNLSGM IPVVVPNLSL DTWQYYTPAY ELDQKILVKA
     AAVRGKWIDQ GQSLNIFLSL DKASGGYLNE IYQLAWELGV KSTYYLRSES PDSEKVNVAD
     RSIECEGCQ
//