ID   A0A2S0PBU4_9NEIS        Unreviewed;       926 AA.
AC   A0A2S0PBU4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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   ORFNames=DAI18_13035 {ECO:0000313|EMBL:AVY94859.1};
OS   Microvirgula aerodenitrificans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Aquaspirillaceae; Microvirgula.
OX   NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY94859.1, ECO:0000313|Proteomes:UP000244173};
RN   [1] {ECO:0000313|EMBL:AVY94859.1, ECO:0000313|Proteomes:UP000244173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BE2.4 {ECO:0000313|EMBL:AVY94859.1,
RC   ECO:0000313|Proteomes:UP000244173};
RA   Anderson E., Jang J., Ishii S.;
RT   "Denitrifier Microvirgula.";
RL   Submitted (APR-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; CP028519; AVY94859.1; -; Genomic_DNA.
DR   RefSeq; WP_028499621.1; NZ_CP028519.1.
DR   AlphaFoldDB; A0A2S0PBU4; -.
DR   STRING; 1122240.GCA_000620105_02621; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000244173; 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; 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:UP000244173}.
FT   DOMAIN          9..109
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
FT   DOMAIN          124..214
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   926 AA;  102460 MW;  42BF3693C47D53C8 CRC64;
     MSVASTASYQ CIRRNGDVVP FAPDKISVAL SKAFLAVLGS EAGGSSRLRD EVEHLTATVV
     AALIRRRPEG GPIHIEDIQD QVELALMRAG EQEVARAYVL YRERRAAERR AAREALGLAA
     APTLHVTRAD GSRAPLDLDR MATLVHTACI GLEADTDPAA ILGDTLKNLY DGVSEAEVGR
     AVVMCARQMI ERDPAYDKVT ARLLLDSIRG EVLGRHVAQT DMAALYADAF PGAIQRGIQA
     ELLDPRLGEF DLARLGQALN ADADLQFGYL GLQTLYDRYF LHIEGRRIEL PQTFFMRVAM
     GLALNEAERN DRAIEFYRVL SSFDFMSSTP TLFNAGTLHS QLSSCYLTTL GDDLTEIFDG
     IKENALLSKY AGGLGNDWTP VRSLGSHIKG TNGKSQGVVP FLKVANDTAV AVNQGGKRKG
     AVCAYLETWH ADIEEFLELR KNTGDDRRRT HDMNTANWVP DLFMQRVMED GPWSLFSPSE
     TPDLHDLTGK AFARRYAEYE AMGERGELRV YKRLRALDLW RKMLTMLFET GHPWLTFKDP
     CNLRSPQQHM GVVHSSNLCT EITLNTSDSE IAVCNLGSVN LANHIRNGQL DDAKLAGTVR
     TAMRMLDNVI DLNFYPVEKA RNANMRHRPV GMGLMGFQDA LHALGLAYGS DAAVEFADRS
     MESIAYHAYW ASTSLAEERG TYQTYDGSLW SRGILPHDSL DLLAESRGGW LEVDRSTTLD
     WDRLRARIKQ FGMRNSNCLA IAPTATIANI IGVSASIEPT YKNLFVKSNL SGEFTVVNEY
     LVRDLKRLGL WDKVMLADLK YFDGDLGPIE RIPAEVKALY ATAFDLDPSW LVEAASRRQK
     WIDQAQSLNL YMAGASGKKL DTLYKHAWVR GLKTTYYLRT LAATSAEKST GRGGELNAVP
     VAAPPAVPAT DMKFCSIDNP DCESCQ
//