ID C3XDX6_9HELI Unreviewed; 785 AA.
AC C3XDX6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=HRAG_00272 {ECO:0000313|EMBL:EEO23215.1};
OS Helicobacter bilis ATCC 43879.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=613026 {ECO:0000313|EMBL:EEO23215.1, ECO:0000313|Proteomes:UP000005085};
RN [1] {ECO:0000313|EMBL:EEO23215.1, ECO:0000313|Proteomes:UP000005085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43879 {ECO:0000313|EMBL:EEO23215.1,
RC ECO:0000313|Proteomes:UP000005085};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(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:EEO23215.1}.
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DR EMBL; ACDN02000006; EEO23215.1; -; Genomic_DNA.
DR RefSeq; WP_005216944.1; NZ_KI392032.1.
DR AlphaFoldDB; C3XDX6; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_7; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000005085; Unassembled WGS sequence.
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:UP000005085}.
FT DOMAIN 4..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 785 AA; 89329 MW; 200F3D138AE7F50D CRC64;
MQTKCVIKRN GSMEELDITK IQKHTSSAVE GLSGTSQSEL EVDAKLQFYD GITTERIQDT
LIKTAVDKID VASPNWTFVA ARLFLYDLYH RVSRFTGYRH LREYFEVGER EGKLLKGLKE
KFDLDLLDSK IVADRDLQFN YLGIKTLYDR YLLKDSNGKP IELPQHMFMA IAMFLAQNEK
DCNEWAIKFY DALSNFEVMC ATPTLSNART TRHQLSSCYI GSTPDNIEGI FDSYKEMALL
SKYGGGIGWD FSQVRTIGSF IDGHKNAAGG IIPFLKITND IAIAVDQLGT RKGAIATYIE
IWHNDVTEFI ELRKNSGEER RRTHDLFPAL WICDLFMERV LQDSQWSFFD PYTCRELTNL
YGDEFKKRYE ELEKMPNMVV SSMPAKDLWK KILNSYFETG LPFLCFKDSA NRANPNAHSG
IIRSSNLCTE IFQNTEPSHY RVEVEFDDGE RIYFEESEEV VVDSGVTKRA NKLTSIDSLK
GKKIFNTQRV QTGGQTAVCN LASINLSKIH THEDIERIVP IAVRMLDNVI DLNFYPSRKV
KVTNMANRAI GLGVMGEAEL LASKLVLWGS EAHFSLIDSI MEAISYNAIK ASAMLAKERG
AYPTYEGSNW SKGIFPIDKA NEKAKAIVER IFHYDWESLR DLVKSEGIRN GYLMAIAPTS
SISILVGTTQ TIEPIYKQIW HEENLSGMIK SVVPNLTLET INFYPSAYSI NQHDLVRAAA
VRQKWIDQGQ SLNIFIRLDS VSGKQLHEIY MLAWSLGLKS TYYLRSQSKE ADDVVDRSME
CVNCQ
//
