ID A0A3D8IVJ9_9HELI Unreviewed; 788 AA.
AC A0A3D8IVJ9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:VEJ24377.1};
GN ORFNames=CQA62_03940 {ECO:0000313|EMBL:RDU69299.1}, NCTC13205_00514
GN {ECO:0000313|EMBL:VEJ24377.1};
OS Helicobacter cholecystus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=45498 {ECO:0000313|EMBL:RDU69299.1, ECO:0000313|Proteomes:UP000257067};
RN [1] {ECO:0000313|EMBL:RDU69299.1, ECO:0000313|Proteomes:UP000257067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700242 {ECO:0000313|EMBL:RDU69299.1,
RC ECO:0000313|Proteomes:UP000257067};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEJ24377.1, ECO:0000313|Proteomes:UP000272814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13205 {ECO:0000313|EMBL:VEJ24377.1,
RC ECO:0000313|Proteomes:UP000272814};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; NXLU01000003; RDU69299.1; -; Genomic_DNA.
DR EMBL; LR134518; VEJ24377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8IVJ9; -.
DR KEGG; hcl:NCTC13205_00514; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000257067; Unassembled WGS sequence.
DR Proteomes; UP000272814; Chromosome 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257067}.
FT DOMAIN 2..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 788 AA; 89691 MW; F4A8122844CBF6F6 CRC64;
MLRVVKRSGR IEALDISKIQ KYTADAVANL EGVSQSELEV DAKLHFKDLI TTEEIQQTLI
KTAVDKIDVD TPNWTFVAAR LFLYDLYHKV SGFTGYKHLK EYFAKGEAEG KILKGFKEKF
DLEYLNEKID PKRDLQFNYL GIKTLYDRYL IKDRNNAPIE LPQQMFMALA MFMAQNEKEP
NEWAVKFYDV ISKFEVVTAT PTLANGRTTR HQLSSCYIGS TPDNIEGIFD AYKEMALLSK
YGGGIGWDFS KVRGLGSFID GHKNAAGGVV PFLKIANDVA IAVDQLGTRK GAIATYLEVW
HTDITDFIDL RKNSGEERRR THDLFPAVWI CDLFMKRVEE NAQWTLFDPY ECKELTELYG
EEFEAKYIEY ENNPHIIKEH ISAKELWKKI LTNYFESGLP FLAFKDNANR ANPNAHAGII
RSSNLCTEIF QNTHPSQYLV EIEFEDGSKE LFEEHEEITT DAGISKKANK LTSIDSLKGK
KIFIAQKIQQ GGLTAVCNLA SINLSKINTK EDIERVLPVA IRILDNVIDL NFYPNRKVRV
TNMQNRAIGL GVMGEAEMLA RENITWGSNE HLERIDEIME MISFNAISAS SDLAKEKGIY
PQFEGSNWSK GIFPIDVASK EALKLVDRGG LFGMTYDWNT LREKVKAQGM RNGYLMAIAP
TSSISILVGT TQTIEPVYKR KWFEENLSGL IPVVVPNLTL ETWNYYVSAY DLDQTDLIRA
AAVRQKWVDQ GQSVNIFMRL DRASGKLLND IYMLAWKLGL KSTYYLRSQS PDAQEQIMDR
SVECVSCQ
//
