ID   A0A191ZJY6_9GAMM        Unreviewed;       936 AA.
AC   A0A191ZJY6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=A9404_01995 {ECO:0000313|EMBL:ANJ68221.1};
OS   Halothiobacillus diazotrophicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=1860122 {ECO:0000313|EMBL:ANJ68221.1, ECO:0000313|Proteomes:UP000078596};
RN   [1] {ECO:0000313|EMBL:ANJ68221.1, ECO:0000313|Proteomes:UP000078596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS2 {ECO:0000313|EMBL:ANJ68221.1,
RC   ECO:0000313|Proteomes:UP000078596};
RA   Luo J., Tan X., Lin W.;
RT   "Insight into the functional genes involving in sulfur oxidation in Pearl
RT   River water.";
RL   Submitted (JUN-2016) 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; CP016027; ANJ68221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A191ZJY6; -.
DR   STRING; 1860122.A9404_01995; -.
DR   KEGG; haz:A9404_01995; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000078596; 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; 2.
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; 2.
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:UP000078596}.
FT   DOMAIN          15..115
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   DOMAIN          129..218
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   936 AA;  104521 MW;  71DE9DE37E3B9668 CRC64;
     MNAEVETAAT TPGSLRVIRR NGKVTAYDAS KIRVAMTKAF LAVEGGGAAV SMRVHDLVAN
     LGDGITQALM RRMPGGGTVH IEDIQDQVEL ALMREGHHKV ARAYVLYREQ QAQKRAAEVK
     EEAEAAPQLH MKRADGTLVP LDQARLRALV DEACAGLSDV DAGAVARETL RNLFDGVPEK
     EVNTALVMSA RTLIEKDPNY SYVAARLLLD GLRTEALRFL KQPVTECTQA EMGNLYADYF
     TAYISAGIEH ELLDPTLKQY DLKRLAAAFE PTRDLQFTYL GLQTLYDRYF LHSRGVRFEL
     PQAFFMRVAM GLAINEIDRE ARAIEFYRLL SSFDFMSSTP TLFNAGTLRP QLSSCYLTTV
     PDDLDGIFAA VKDNALLSKF AGGLGNDWTR VRALGAHIKG TNGQSQGVVP FLKVANDTAV
     AVNQGGKRKG AVCAYLETWH MDIEEFLDLR KNTGDDRRRT HDMNTANWVP DLFMQRVIEE
     GDWTLFSPSD VPDLHDLTGE AFTKAYTRYE EMADRGDLKH FRRVKAVTLW RKMLGMLFET
     GHPWITFKDP CNIRYTNQHA GVVHSSNLCT EITLHTNDNE IAVCNLGSVN LAQHVTADGL
     DQEKLARTIQ TAMRMLDNVI EYNYYSVPQA RNSNLRHRPV GLGIMGFQDA LHIQKIPYSS
     DAAVEFADRS MEAVSYHAIS ASSDLARERG RYASYEGSLW SRGILPIDSI ELLAQARGKY
     LVMNRDTSLD WDSLREKVRT QGMRNSNTMA IAPTATISNI CGVAQSIEPT FENLFVKSNL
     SGEFTVVNPY LVRDLKAKGL WDEVMVNDLK YFDGSVQEID RIPADIKALY ATAFEVEPRW
     LIEAASRRQK WLDQAQSLNL YLADPSGPKL DQMYKNAWLV GLKTTYYLRA ASKTRVEKTT
     MTKLDGKLRG VSADVMPASA EPKACLIDDP GCEACQ
//