ID   RIR1_CHLMU              Reviewed;        1047 AA.
AC   Q9PL93;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase;
GN   Name=nrdA; OrderedLocusNames=TC_0214;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39086.1; -; Genomic_DNA.
DR   PIR; F81728; F81728.
DR   RefSeq; WP_010229837.1; NZ_CP063055.1.
DR   AlphaFoldDB; Q9PL93; -.
DR   SMR; Q9PL93; -.
DR   GeneID; 1246340; -.
DR   KEGG; cmu:TC_0214; -.
DR   eggNOG; COG0209; Bacteria.
DR   eggNOG; COG1327; Bacteria.
DR   HOGENOM; CLU_000404_3_0_0; -.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; Repeat.
FT   CHAIN           1..1047
FT                   /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT                   /id="PRO_0000187210"
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;  120036 MW;  9B3FFD9BFAF817AA CRC64;
     MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL ENSIRSITHQ
     VVKEVVQKIT DGQVVTVERI QDMVESQLYI NGLQDVARDY VVYRDDRKAH REKSWQSLSV
     IRRCGTTVHF NPMKISAALE KAFRATDRIE GMTPDFVREE VNALTQKIVA EIEERCSQQD
     SRIDIEQIQD IVEQQLMVVG HYATAKNYIL YREARARVRD NRVEDQIVEE APSEETFEVL
     SKDGSTYMIT HSQLLARLAR ACSRFPETTD AALLTDMAFS NFYSGIKESE VVLACIMAAR
     ANIEKEPDYA FVAAELLLDV VYKEALDRSR GDEDLEQVYR DHFKRYIMEG DSYRLNPELK
     NLFDLDALAN AMDLSRDLQF SYMGIQNLYD RYFNHDDGRR LETPQIFWMR VAMGLALKEQ
     DKTYWAITFY NLLSTFRYTP ATPTLFNSGM RHSQLSSCYL STVQDDLVNI YKVISDNAML
     SKWAGGIGND WTAIRATGAL IKGTNGKSQG VIPFIKVTND TAVAVNQGGK RKGAVCVYLE
     VWHLDYEDFL ELRKNTGDDR RRAHDVNTAS WIPDLFFKRL QQKGSWTLFS PDDVPGLHDA
     YGEEFERLYE EYERKVDSGE IRLYKKVEAE DLWRKMLSML FETGHPWMTF KDPSNIRSAQ
     DHTGVVRCSN LCTEILLNCS ETETAVCNLG SVNLVQHILD DGLDEEKLSE TISIAVRMLD
     NVIDINFYPT KEAKEANFAH RAIGLGVMGF QDALYKLDIS YASQEAVEFA DYSSELISYY
     AIQASCLLAK ERGTYSSYKG SKWDRGLLPI DTIQLLANYR GKDNLQMDTS VRKDWEPIRS
     LIREHGMRNC QLMAIAPTAT ISNIIGVTQS IEPTYKHLFV KSNLSGEFTI PNVYLIEKLK
     KLGIWDADML DDLKYFDGSL LEIERVPDHI KHIFLTAFEI EPEWILECAS RRQKWIDMGQ
     SLNLYLAQPD GKKLSNMYLT AWKKGLKTTY YLRSSSATTV EKSFVDINKR GIQPRWMKNK
     SASAGIVVER ASKTPVCSLE EGCEVCQ
//