Skip Header

Contribute Send feedback
Read comments (?) or add your own

O84834 (RIR1_CHLTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. 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
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:CT_827
OrganismChlamydia trachomatis (strain D/UW-3/Cx) [Reference proteome] [HAMAP]
Taxonomic identifier272561 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia ›

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10471047Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187212

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
O84834 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: A3658C187B4668AE

FASTA1,047119,421
        10         20         30         40         50         60 
MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL ESSIRSITHQ 

        70         80         90        100        110        120 
VVKEVVQKIT DGQVVTVERI QDMVESQLYV NGLQDVARDY IVYRDDRKAH RKKSWQSLSV 

       130        140        150        160        170        180 
VRRCGTVVHF NPMKISAALE KAFRATDKTE GMTPSSVREE INALTQNIVA EIEECCPQQD 

       190        200        210        220        230        240 
RRIDIEKIQD IVEQQLMVVG HYAVAKNYIL YREARARVRD NREEDGSTEK TIAEEAVEVL 

       250        260        270        280        290        300 
SKDGSTYTMT HSQLLAHLAR ACSRFPETTD AALLTDMAFA NFYSGIKESE VVLACIMAAR 

       310        320        330        340        350        360 
ANIEKEPDYA FVAAELLLDV VYKEALGKSK YAEDLEQAHR DHFKRYIAEG DTYRLNAELK 

       370        380        390        400        410        420 
HLFDLDALAD AMDLSRDLQF SYMGIQNLYD RYFNHHEGCR LETPQIFWMR VAMGLALNEQ 

       430        440        450        460        470        480 
DKTSWAITFY NLLSTFRYTP ATPTLFNSGM RHSQLSSCYL STVQDNLVNI YKVIADNAML 

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

       550        560        570        580        590        600 
VWHLDYEDFL ELRKNTGDER RRAHDVNIAS WIPDLFFKRL QQKGTWTLFS PDDVPGLHDA 

       610        620        630        640        650        660 
YGEEFERLYE EYERKVDTGE IRLFKKVEAE DLWRKMLSML FETGHPWMTF KDPSNIRSAQ 

       670        680        690        700        710        720 
DHKGVVRCSN LCTEILLNCS ETETAVCNLG SINLVQHIVG DGLDEEKLSE TISIAVRMLD 

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

       790        800        810        820        830        840 
AIQASCLLAK ERGTYSSYKG SKWDRGLLPI DTIQLLANYR GEANLQMDTS SRKDWEPIRS 

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

       910        920        930        940        950        960 
KLGIWDADML DDLKYFDGSL LEIERIPDHL KHIFLTAFEI EPEWIIECAS RRQKWIDMGQ 

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

      1030       1040 
SASAGIIVER AKKAPVCSLE EGCEACQ

« Hide

References

[1]"Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis."
Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.
Science 282:754-759(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D/UW-3/Cx.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001273 Genomic DNA. Translation: AAC68424.2.
PIRD71466.
RefSeqNP_220348.1. NC_000117.1.

3D structure databases

ProteinModelPortalO84834.
ModBaseSearch...

Protein-protein interaction databases

STRING272561.CT827.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC68424; AAC68424; CT_827.
GeneID884629.
KEGGctr:CT827.
PATRIC20381366. VBIChlTra43535_0913.

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMAPQARNSN.
ProtClustDBPRK12365.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15783.
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. Ribonucleo_red_N. 1 hit.
TIGRFAMsTIGR02506. NrdE_NrdA. 1 hit.
PROSITEPS51161. ATP_CONE. 3 hits.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_CHLTR
AccessionPrimary (citable) accession number: O84834
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents