ID RIR1_CHLTR Reviewed; 1047 AA. AC O84834; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 131. DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Ribonucleotide reductase; GN Name=nrdA; OrderedLocusNames=CT_827; OS Chlamydia trachomatis (strain D/UW-3/Cx). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=272561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=D/UW-3/Cx; RX PubMed=9784136; DOI=10.1126/science.282.5389.754; RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.; RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia RT trachomatis."; RL Science 282:754-759(1998). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides (By similarity). {ECO:0000250}. 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 -!- ACTIVITY REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding. The type of nucleotide CC bound at the specificity site determines substrate preference. It seems CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP CC reduction and dTTP favors GDP reduction (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain 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; AE001273; AAC68424.2; -; Genomic_DNA. DR PIR; D71466; D71466. DR RefSeq; NP_220348.1; NC_000117.1. DR RefSeq; WP_009872213.1; NC_000117.1. DR AlphaFoldDB; O84834; -. DR SMR; O84834; -. DR STRING; 272561.CT_827; -. DR EnsemblBacteria; AAC68424; AAC68424; CT_827. DR GeneID; 884629; -. DR KEGG; ctr:CT_827; -. DR PATRIC; fig|272561.5.peg.913; -. DR HOGENOM; CLU_000404_3_0_0; -. DR InParanoid; O84834; -. DR OrthoDB; 9762933at2; -. DR BioCyc; MetaCyc:MONOMER-15783; -. DR Proteomes; UP000000431; Chromosome. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central. 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; 3. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 3: Inferred from homology; KW Allosteric enzyme; ATP-binding; Deoxyribonucleotide synthesis; KW Disulfide bond; Nucleotide-binding; Oxidoreductase; Reference proteome; KW Repeat. FT CHAIN 1..1047 FT /note="Ribonucleoside-diphosphate reductase subunit alpha" FT /id="PRO_0000187212" FT DOMAIN 9..111 FT /note="ATP-cone 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT DOMAIN 118..219 FT /note="ATP-cone 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT DOMAIN 237..327 FT /note="ATP-cone 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT ACT_SITE 670 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 672 FT /note="Cysteine radical intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 674 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 442 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 457..458 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 486 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 670..674 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 857..861 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 458 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 465 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 495 FT /note="Allosteric effector binding" FT /evidence="ECO:0000250" FT SITE 687 FT /note="Important for hydrogen atom transfer" FT /evidence="ECO:0000250" FT SITE 990 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 991 FT /note="Important for electron transfer" FT /evidence="ECO:0000250" FT SITE 1043 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT SITE 1046 FT /note="Interacts with thioredoxin/glutaredoxin" FT /evidence="ECO:0000250" FT DISULFID 458..687 FT /note="Redox-active" FT /evidence="ECO:0000250" SQ SEQUENCE 1047 AA; 119421 MW; A3658C187B4668AE CRC64; MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL ESSIRSITHQ VVKEVVQKIT DGQVVTVERI QDMVESQLYV NGLQDVARDY IVYRDDRKAH RKKSWQSLSV VRRCGTVVHF NPMKISAALE KAFRATDKTE GMTPSSVREE INALTQNIVA EIEECCPQQD RRIDIEKIQD IVEQQLMVVG HYAVAKNYIL YREARARVRD NREEDGSTEK TIAEEAVEVL SKDGSTYTMT HSQLLAHLAR ACSRFPETTD AALLTDMAFA NFYSGIKESE VVLACIMAAR ANIEKEPDYA FVAAELLLDV VYKEALGKSK YAEDLEQAHR DHFKRYIAEG DTYRLNAELK HLFDLDALAD AMDLSRDLQF SYMGIQNLYD RYFNHHEGCR LETPQIFWMR VAMGLALNEQ DKTSWAITFY NLLSTFRYTP ATPTLFNSGM RHSQLSSCYL STVQDNLVNI YKVIADNAML SKWAGGIGND WTAIRATGAL IKGTNGRSQG VIPFIKVTND TAVAVNQGGK RKGAVCVYLE VWHLDYEDFL ELRKNTGDER RRAHDVNIAS WIPDLFFKRL QQKGTWTLFS PDDVPGLHDA YGEEFERLYE EYERKVDTGE IRLFKKVEAE DLWRKMLSML FETGHPWMTF KDPSNIRSAQ DHKGVVRCSN LCTEILLNCS ETETAVCNLG SINLVQHIVG DGLDEEKLSE TISIAVRMLD NVIDINFYPT KEAKEANFAH RAIGLGVMGF QDALYKLDIS YASQEAVEFA DYSSELISYY AIQASCLLAK ERGTYSSYKG SKWDRGLLPI DTIQLLANYR GEANLQMDTS SRKDWEPIRS LVKEHGMRHC QLMAIAPTAT ISNIIGVTQS IEPTYKHLFV KSNLSGEFTI PNVYLIEKLK KLGIWDADML DDLKYFDGSL LEIERIPDHL KHIFLTAFEI EPEWIIECAS RRQKWIDMGQ SLNLYLAQPD GKKLSNMYLT AWKKGLKTTY YLRSSSATTV EKSFVDINKR GIQPRWMKNK SASAGIIVER AKKAPVCSLE EGCEACQ //