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Q9Z6S5 (RIR1_CHLPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase subunit alpha

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase
Gene names
Name:nrdA
Ordered Locus Names:CPn_0984, CP_0872, CpB1021
OrganismChlamydia pneumoniae (Chlamydophila pneumoniae) [Complete proteome] [HAMAP]
Taxonomic identifier83558 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length1044 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.

Catalytic activity

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.

Enzyme regulation

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase large chain family.

Contains 3 ATP-cone domains.

Ontologies

Keywords
   Biological processDNA replication
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentribonucleoside-diphosphate reductase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10441044Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187211

Regions

Domain9 – 111103ATP-cone 1
Domain118 – 217100ATP-cone 2
Domain235 – 32591ATP-cone 3
Region455 – 4562Substrate binding By similarity
Region668 – 6725Substrate binding By similarity
Region855 – 8595Substrate binding By similarity

Sites

Active site6681Proton acceptor By similarity
Active site6701Cysteine radical intermediate By similarity
Active site6721Proton acceptor By similarity
Binding site4401Substrate By similarity
Binding site4841Substrate; via amide nitrogen By similarity
Site4561Important for hydrogen atom transfer By similarity
Site4631Allosteric effector binding By similarity
Site4931Allosteric effector binding By similarity
Site6851Important for hydrogen atom transfer By similarity
Site9881Important for electron transfer By similarity
Site9891Important for electron transfer By similarity
Site10401Interacts with thioredoxin/glutaredoxin By similarity
Site10431Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond456 ↔ 685Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z6S5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 0A7379FA01B7372E

FASTA1,044119,399
        10         20         30         40         50         60 
MVEVEEKHYT IVKRNGMFVP FNQDRIFQAL EAAFRDTRSL ETSSPLPKDL EESIAQITHK 

        70         80         90        100        110        120 
VVKEVLAKIS EGQVVTVERI QDLVESQLYI SGLQDVARDY IVYRDQRKAE RGNSSSIIAI 

       130        140        150        160        170        180 
IRRDGGSAKF NPMKISAALE KAFRATLQIN GMTPPATLSE INDLTLRIVE DVLSLHGEEA 

       190        200        210        220        230        240 
INLEEIQDIV EKQLMVAGYY DVAKNYILYR EARARARANK DQDGQEEFVP QEETYVVQKE 

       250        260        270        280        290        300 
DGTTYLLRKT DLEKRFSWAC KRFPKTTDSQ LLADMAFMNL YSGIKEDEVT TACIMAARAN 

       310        320        330        340        350        360 
IEREPDYAFI AAELLTSSLY EETLGCSSQD PNLSEIHKKH FKEYILNGEE YRLNPQLKDY 

       370        380        390        400        410        420 
DLDALSEVLD LSRDQQFSYM GVQNLYDRYF NLHEGRRLET AQIFWMRVSM GLALNEGEQK 

       430        440        450        460        470        480 
NFWAITFYNL LSTFRYTPAT PTLFNSGMRH SQLSSCYLST VKDDLSHIYK VISDNALLSK 

       490        500        510        520        530        540 
WAGGIGNDWT DVRATGAVIK GTNGKSQGVI PFIKVANDTA IAVNQGGKRK GAMCVYLENW 

       550        560        570        580        590        600 
HLDYEDFLEL RKNTGDERRR THDINTASWI PDLFFKRLEK KGMWTLFSPD DVPGLHEAYG 

       610        620        630        640        650        660 
LEFEKLYEEY ERKVESGEIR LYKKVEAEVL WRKMLSMLYE TGHPWITFKD PSNIRSNQDH 

       670        680        690        700        710        720 
VGVVRCSNLC TEILLNCSES ETAVCNLGSI NLVEHIRNDK LDEEKLKETI SIAIRILDNV 

       730        740        750        760        770        780 
IDLNFYPTPE AKQANLTHRA VGLGVMGFQD VLYELNISYA SQEAVEFSDE CSEIIAYYAI 

       790        800        810        820        830        840 
LASSLLAKER GTYASYSGSK WDRGYLPLDT IELLKETRGE HNVLVDTSSK KDWTPVRDTI 

       850        860        870        880        890        900 
QKYGMRNSQV MAIAPTATIS NIIGVTQSIE PMYKHLFVKS NLSGEFTIPN TYLIKKLKEL 

       910        920        930        940        950        960 
GLWDAEMLDD LKYFDGSLLE IERIPNHLKK LFLTAFEIEP EWIIECTSRR QKWIDMGVSL 

       970        980        990       1000       1010       1020 
NLYLAEPDGK KLSNMYLTAW KKGLKTTYYL RSQAATSVEK SFIDINKRGI QPRWMKNKSA 

      1030       1040 
STSIVVERKT TPVCSMEEGC ESCQ 

« Hide

References

[1]"Comparative genomes of Chlamydia pneumoniae and C. trachomatis."
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.
Nat. Genet. 21:385-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CWL029.
[2]"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. expand/collapse author list , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AR39.
[3]"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J138.
[4]"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001363 Genomic DNA. Translation: AAD19121.1.
AE002161 Genomic DNA. Translation: AAF38661.1.
BA000008 Genomic DNA. Translation: BAA99191.1.
AE009440 Genomic DNA. Translation: AAP98950.1.
PIRA72010.
E86613.
RefSeqNP_225178.1. NC_000922.1.
NP_301039.1. NC_002491.1.
NP_445410.1. NC_002179.2.
NP_877293.1. NC_005043.1.

3D structure databases

ProteinModelPortalQ9Z6S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING115713.CPn0984.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD19121; AAD19121; CPn_0984.
AAF38661; AAF38661; CP_0872.
AAP98950; AAP98950; CpB1021.
BAA99191; BAA99191; BAA99191.
GeneID1467700.
895606.
919750.
963324.
KEGGcpa:CP0872.
cpj:CPj0984.
cpn:CPn0984.
cpt:CpB1021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
HOGENOMHOG000057036.
KOK00525.
OMAEACLMCQ.
OrthoDBEOG6J48HC.

Enzyme and pathway databases

BioCycCPNE115711:GI7B-901-MONOMER.
CPNE115713:GHEY-1026-MONOMER.
CPNE138677:GH8N-1016-MONOMER.
CPNE182082:GH4N-1054-MONOMER.
UniPathwayUPA00326.

Family and domain databases

InterProIPR005144. ATP-cone.
IPR013346. NrdE_NrdA.
IPR000788. RNR_lg_C.
IPR013509. RNR_lsu_N.
IPR008926. RNR_R1-su_N.
[Graphical view]
PfamPF03477. ATP-cone. 3 hits.
PF02867. Ribonuc_red_lgC. 1 hit.
PF00317. Ribonuc_red_lgN. 1 hit.
[Graphical view]
PRINTSPR01183. RIBORDTASEM1.
SUPFAMSSF48168. SSF48168. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 3 hits.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_CHLPN
AccessionPrimary (citable) accession number: Q9Z6S5
Secondary accession number(s): Q9JQC5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways