ID   I0EN25_HELC0            Unreviewed;       788 AA.
AC   I0EN25;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=HCW_05410 {ECO:0000313|EMBL:AFI04344.1};
OS   Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI04344.1, ECO:0000313|Proteomes:UP000005010};
RN   [1] {ECO:0000313|Proteomes:UP000005010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA   Kersulyte D., Berg D.E.;
RT   "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL   Submitted (APR-2012) 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}.
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DR   EMBL; CP003479; AFI04344.1; -; Genomic_DNA.
DR   RefSeq; WP_014661214.1; NC_017737.1.
DR   AlphaFoldDB; I0EN25; -.
DR   STRING; 182217.HCW_05410; -.
DR   KEGG; hce:HCW_05410; -.
DR   PATRIC; fig|182217.3.peg.1149; -.
DR   eggNOG; COG0209; Bacteria.
DR   HOGENOM; CLU_000404_3_0_7; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000005010; Chromosome.
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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; 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   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}.
FT   DOMAIN          2..92
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   788 AA;  90419 MW;  080114AA11379692 CRC64;
     MITVTKRNGR IEPLDITKIQ KYTKDATENL EGVSQSELEV DARLQFRDKI TTEEIQQTLI
     KTAVDKIDID TPNWSFVASR LFLYDLYHKV SGFTGYKHLK EYFENAEEKN RMLKGFKEKF
     DLEFLNSQIK PERDFQFNYL GIKTLYDRYL LKDTDNNPIE LPQHMFMSIA MFLAQNEEEP
     NKIALEFYEV LSKFEAMCAT PTLANARTTK HQLSSCYIGS TPDNIEGIFD SYKEMALLSK
     YGGGIGWDFS LVRSIGSYID GHKNASAGTI PFLKIANDVA IAVDQLGTRK GAIAVYLEIW
     HIDVMEFIDL RKNSGDERRR AHDLFPALWV CDLFMKRVLE DAMWTLFDPY ECKDLAELYG
     EEFEKRYLEY EKNPTIIKEY INAKDLWKKV LMNYFEAGLP FLAFKDNANR CNPNAHAGII
     RSSNLCTEIF QNTAPNHYYM QVEYTDGTIE FFEEKELVTT DSHITKYANK LTSTDTLKGK
     QIYIATKVAK DGQTAVCNLA SINLSKINTE EDIKRVVPIM VRLLDNVIDL NFYPNRKVKA
     TNLQNRAIGL GVMGEAQMLA ENKIAWGSKE HLEKIDCLME QISYYAIDTS ANLAKEKGVY
     KDFEGSEWSK GIFPIDKANK EALKLTERGL FDYTCDWQSL KEKVKANGMR NGYLMAIAPT
     SSISILVGTT QTIEPIYKKK WFEENLSGLI PVVVPNLSLE TWNFYTSAYD IDAKDLIKVA
     AVRQKWIDQG QSTNVFLRIE SASGKTLHEI YTLAWRLGLK STYYLRSESP TLDEKSVLDR
     SIECHNCQ
//