ID NRDD_HAEIN Reviewed; 707 AA. AC P43752; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Anaerobic ribonucleoside-triphosphate reductase {ECO:0000250|UniProtKB:P28903}; DE EC=1.1.98.6 {ECO:0000250|UniProtKB:P28903}; DE AltName: Full=Class III ribonucleoside-triphosphate reductase {ECO:0000250|UniProtKB:P28903}; GN Name=nrdD; OrderedLocusNames=HI_0075; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the conversion of ribonucleotides into CC deoxyribonucleotides, which are required for DNA synthesis and repair. CC {ECO:0000250|UniProtKB:P28903}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'- CC deoxyribonucleoside 5'-triphosphate + CO2 + H2O; CC Xref=Rhea:RHEA:51476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:61557, CC ChEBI:CHEBI:61560; EC=1.1.98.6; CC Evidence={ECO:0000250|UniProtKB:P28903}; CC -!- ACTIVITY REGULATION: Activated under anaerobic conditions by NrdG, a CC tightly associated activase. Activation involves the formation of a CC glycyl radical at Gly-682. {ECO:0000250|UniProtKB:P28903}. CC -!- SUBUNIT: Forms a tetramer composed of two NrdD and two NrdG subunits. CC {ECO:0000250|UniProtKB:P28903}. CC -!- SIMILARITY: Belongs to the anaerobic ribonucleoside-triphosphate CC reductase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC21751.1; -; Genomic_DNA. DR PIR; A64047; A64047. DR RefSeq; NP_438248.1; NC_000907.1. DR AlphaFoldDB; P43752; -. DR SMR; P43752; -. DR STRING; 71421.HI_0075; -. DR EnsemblBacteria; AAC21751; AAC21751; HI_0075. DR KEGG; hin:HI_0075; -. DR PATRIC; fig|71421.8.peg.76; -. DR eggNOG; COG1327; Bacteria. DR eggNOG; COG1328; Bacteria. DR HOGENOM; CLU_002707_2_0_6; -. DR OrthoDB; 9804622at2; -. DR PhylomeDB; P43752; -. DR BioCyc; HINF71421:G1GJ1-76-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0031250; C:anaerobic ribonucleoside-triphosphate reductase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IBA:GO_Central. DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR CDD; cd01675; RNR_III; 1. DR Gene3D; 3.20.70.20; -; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR019777; Form_AcTrfase_GR_CS. DR InterPro; IPR001150; Gly_radical. DR InterPro; IPR012833; NrdD. DR NCBIfam; TIGR02487; NrdD; 1. DR PANTHER; PTHR21075; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1. DR PANTHER; PTHR21075:SF0; ANAEROBIC RIBONUCLEOSIDE-TRIPHOSPHATE REDUCTASE; 1. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF13597; NRDD; 1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00850; GLY_RADICAL_1; 1. DR PROSITE; PS51149; GLY_RADICAL_2; 1. PE 3: Inferred from homology; KW ATP-binding; Metal-binding; Nucleotide-binding; Organic radical; KW Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..707 FT /note="Anaerobic ribonucleoside-triphosphate reductase" FT /id="PRO_0000166684" FT DOMAIN 4..95 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT DOMAIN 584..707 FT /note="Glycine radical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493" FT BINDING 645 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07071" FT BINDING 648 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07071" FT BINDING 663 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07071" FT BINDING 666 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P07071" FT MOD_RES 682 FT /note="Glycine radical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493" SQ SEQUENCE 707 AA; 80233 MW; A3795F7921A6781D CRC64; MSNFGVIKRD GSRAEFEIQR IINAIKKAAS AVNISDEFYC HQIGQEVGNE IFTRHQGEID INQIQKIVED KLMASRYPEV ARAYIEYRHD RDLAREKRSQ LTKEIEGLIE QSNVELLNEN ANKDAKVIPT QRDLLAGIVA KHYAKHNILP RDVVEAHEKG EIHYHDLDYA PFFPMFNCML VDLEGMLSRG FKMGNAEIEP PKSIGTATAV TAQIIAQVAS HIYGGTTINR IDEVLSPYVQ ISYEKHLKHA QEWNVPDVEG YAKALIEKEC FDAFQSLEYE VNTLHTSNGQ TPFVTFGFGL GTSWQSRLIQ QAILKNRIRG LGKNHKTPVF PKLVFTIKKG LNQNKGDPNY DIKQLALECA SKRMYPDILN YDQVVKVTGS FKAPMGCRSF LGAYEEKGHE IHDGRNNLGV VSLNLPRIAL ESKNEEDFYR TLDERLAIAK KALMTRIARL ENTKARVAPI LYMEGACGVR LKADENVAQI FKNGRASISL GYIGIHETIN ALYNKGHIFD DEQLREKGIA IVRHLSEAVK RWQKETGYAF SLYSTPSENL CDRFCRLDTK KFGVIEGVTD KGYYTNSYHL DVEKKVNPYD KLDFEMTYPP LASGGFICYG EYPNIQHNLK ALEDVWDYSY DRVPYYGTNT PIDECYECGF TGEFECTSKG FVCPKCGNHD STKVSVTRRV CGYLGSPDAR PFNAGKQEEV KRRVKHL //