RIR1_CHLPN
ID RIR1_CHLPN Reviewed; 1044 AA.
AC Q9Z6S5; Q9JQC5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit alpha;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase;
GN Name=nrdA; OrderedLocusNames=CPn_0984, CP_0872, CpB1021;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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 (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 -!- PATHWAY: Genetic information processing; DNA replication.
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}.
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DR EMBL; AE001363; AAD19121.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38661.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99191.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98950.1; -; Genomic_DNA.
DR PIR; A72010; A72010.
DR PIR; E86613; E86613.
DR RefSeq; NP_225178.1; NC_000922.1.
DR RefSeq; WP_010883617.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6S5; -.
DR SMR; Q9Z6S5; -.
DR STRING; 115711.CP_0872; -.
DR PRIDE; Q9Z6S5; -.
DR EnsemblBacteria; AAD19121; AAD19121; CPn_0984.
DR EnsemblBacteria; AAF38661; AAF38661; CP_0872.
DR GeneID; 45051040; -.
DR KEGG; cpa:CP_0872; -.
DR KEGG; cpj:nrdA; -.
DR KEGG; cpn:CPn_0984; -.
DR KEGG; cpt:CpB1021; -.
DR PATRIC; fig|115713.3.peg.1079; -.
DR eggNOG; COG0209; Bacteria.
DR eggNOG; COG1327; Bacteria.
DR HOGENOM; CLU_000404_3_0_0; -.
DR OrthoDB; 357568at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; PTHR11573; 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; SSF48168; SSF48168; 1.
DR TIGRFAMs; TIGR02506; NrdE_NrdA; 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..1044
FT /note="Ribonucleoside-diphosphate reductase subunit alpha"
FT /id="PRO_0000187211"
FT DOMAIN 9..111
FT /note="ATP-cone 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT DOMAIN 118..217
FT /note="ATP-cone 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT DOMAIN 235..325
FT /note="ATP-cone 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492"
FT ACT_SITE 668
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 670
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 672
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 455..456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 668..672
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 855..859
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 456
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 463
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 493
FT /note="Allosteric effector binding"
FT /evidence="ECO:0000250"
FT SITE 685
FT /note="Important for hydrogen atom transfer"
FT /evidence="ECO:0000250"
FT SITE 988
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 989
FT /note="Important for electron transfer"
FT /evidence="ECO:0000250"
FT SITE 1040
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT SITE 1043
FT /note="Interacts with thioredoxin/glutaredoxin"
FT /evidence="ECO:0000250"
FT DISULFID 456..685
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1044 AA; 119399 MW; 0A7379FA01B7372E CRC64;
MVEVEEKHYT IVKRNGMFVP FNQDRIFQAL EAAFRDTRSL ETSSPLPKDL EESIAQITHK
VVKEVLAKIS EGQVVTVERI QDLVESQLYI SGLQDVARDY IVYRDQRKAE RGNSSSIIAI
IRRDGGSAKF NPMKISAALE KAFRATLQIN GMTPPATLSE INDLTLRIVE DVLSLHGEEA
INLEEIQDIV EKQLMVAGYY DVAKNYILYR EARARARANK DQDGQEEFVP QEETYVVQKE
DGTTYLLRKT DLEKRFSWAC KRFPKTTDSQ LLADMAFMNL YSGIKEDEVT TACIMAARAN
IEREPDYAFI AAELLTSSLY EETLGCSSQD PNLSEIHKKH FKEYILNGEE YRLNPQLKDY
DLDALSEVLD LSRDQQFSYM GVQNLYDRYF NLHEGRRLET AQIFWMRVSM GLALNEGEQK
NFWAITFYNL LSTFRYTPAT PTLFNSGMRH SQLSSCYLST VKDDLSHIYK VISDNALLSK
WAGGIGNDWT DVRATGAVIK GTNGKSQGVI PFIKVANDTA IAVNQGGKRK GAMCVYLENW
HLDYEDFLEL RKNTGDERRR THDINTASWI PDLFFKRLEK KGMWTLFSPD DVPGLHEAYG
LEFEKLYEEY ERKVESGEIR LYKKVEAEVL WRKMLSMLYE TGHPWITFKD PSNIRSNQDH
VGVVRCSNLC TEILLNCSES ETAVCNLGSI NLVEHIRNDK LDEEKLKETI SIAIRILDNV
IDLNFYPTPE AKQANLTHRA VGLGVMGFQD VLYELNISYA SQEAVEFSDE CSEIIAYYAI
LASSLLAKER GTYASYSGSK WDRGYLPLDT IELLKETRGE HNVLVDTSSK KDWTPVRDTI
QKYGMRNSQV MAIAPTATIS NIIGVTQSIE PMYKHLFVKS NLSGEFTIPN TYLIKKLKEL
GLWDAEMLDD LKYFDGSLLE IERIPNHLKK LFLTAFEIEP EWIIECTSRR QKWIDMGVSL
NLYLAEPDGK KLSNMYLTAW KKGLKTTYYL RSQAATSVEK SFIDINKRGI QPRWMKNKSA
STSIVVERKT TPVCSMEEGC ESCQ
