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Q9PL93 (RIR1_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. 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:TC_0214
OrganismChlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]
Taxonomic identifier243161 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length1047 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 – 10471047Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187210

Regions

Domain9 – 111103ATP-cone 1
Domain118 – 219102ATP-cone 2
Domain237 – 32791ATP-cone 3
Region457 – 4582Substrate binding By similarity
Region670 – 6745Substrate binding By similarity
Region857 – 8615Substrate binding By similarity

Sites

Active site6701Proton acceptor By similarity
Active site6721Cysteine radical intermediate By similarity
Active site6741Proton acceptor By similarity
Binding site4421Substrate By similarity
Binding site4861Substrate; via amide nitrogen By similarity
Site4581Important for hydrogen atom transfer By similarity
Site4651Allosteric effector binding By similarity
Site4951Allosteric effector binding By similarity
Site6871Important for hydrogen atom transfer By similarity
Site9901Important for electron transfer By similarity
Site9911Important for electron transfer By similarity
Site10431Interacts with thioredoxin/glutaredoxin By similarity
Site10461Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond458 ↔ 687Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PL93 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9B3FFD9BFAF817AA

FASTA1,047120,036
        10         20         30         40         50         60 
MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL ENSIRSITHQ 

        70         80         90        100        110        120 
VVKEVVQKIT DGQVVTVERI QDMVESQLYI NGLQDVARDY VVYRDDRKAH REKSWQSLSV 

       130        140        150        160        170        180 
IRRCGTTVHF NPMKISAALE KAFRATDRIE GMTPDFVREE VNALTQKIVA EIEERCSQQD 

       190        200        210        220        230        240 
SRIDIEQIQD IVEQQLMVVG HYATAKNYIL YREARARVRD NRVEDQIVEE APSEETFEVL 

       250        260        270        280        290        300 
SKDGSTYMIT HSQLLARLAR ACSRFPETTD AALLTDMAFS NFYSGIKESE VVLACIMAAR 

       310        320        330        340        350        360 
ANIEKEPDYA FVAAELLLDV VYKEALDRSR GDEDLEQVYR DHFKRYIMEG DSYRLNPELK 

       370        380        390        400        410        420 
NLFDLDALAN AMDLSRDLQF SYMGIQNLYD RYFNHDDGRR LETPQIFWMR VAMGLALKEQ 

       430        440        450        460        470        480 
DKTYWAITFY NLLSTFRYTP ATPTLFNSGM RHSQLSSCYL STVQDDLVNI YKVISDNAML 

       490        500        510        520        530        540 
SKWAGGIGND WTAIRATGAL IKGTNGKSQG VIPFIKVTND TAVAVNQGGK RKGAVCVYLE 

       550        560        570        580        590        600 
VWHLDYEDFL ELRKNTGDDR RRAHDVNTAS WIPDLFFKRL QQKGSWTLFS PDDVPGLHDA 

       610        620        630        640        650        660 
YGEEFERLYE EYERKVDSGE IRLYKKVEAE DLWRKMLSML FETGHPWMTF KDPSNIRSAQ 

       670        680        690        700        710        720 
DHTGVVRCSN LCTEILLNCS ETETAVCNLG SVNLVQHILD DGLDEEKLSE TISIAVRMLD 

       730        740        750        760        770        780 
NVIDINFYPT KEAKEANFAH RAIGLGVMGF QDALYKLDIS YASQEAVEFA DYSSELISYY 

       790        800        810        820        830        840 
AIQASCLLAK ERGTYSSYKG SKWDRGLLPI DTIQLLANYR GKDNLQMDTS VRKDWEPIRS 

       850        860        870        880        890        900 
LIREHGMRNC QLMAIAPTAT ISNIIGVTQS IEPTYKHLFV KSNLSGEFTI PNVYLIEKLK 

       910        920        930        940        950        960 
KLGIWDADML DDLKYFDGSL LEIERVPDHI KHIFLTAFEI EPEWILECAS RRQKWIDMGQ 

       970        980        990       1000       1010       1020 
SLNLYLAQPD GKKLSNMYLT AWKKGLKTTY YLRSSSATTV EKSFVDINKR GIQPRWMKNK 

      1030       1040 
SASAGIVVER ASKTPVCSLE EGCEVCQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39086.1.
PIRF81728.
RefSeqNP_296593.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PL93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243161.TC0214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF39086; AAF39086; TC_0214.
GeneID1246340.
KEGGcmu:TC_0214.
PATRIC20371810. VBIChlMur19118_0234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMAANGSIQH.
OrthoDBEOG6J48HC.

Enzyme and pathway databases

BioCycCMUR243161:GHYU-225-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. 2 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_CHLMU
AccessionPrimary (citable) accession number: Q9PL93
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 96 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