Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O83972 (RIR1_TREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 99. 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:TP_1008
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length845 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 1 ATP-cone domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187223

Regions

Domain1 – 9898ATP-cone
Region318 – 3192Substrate binding By similarity
Region534 – 5385Substrate binding By similarity
Region725 – 7295Substrate binding By similarity

Sites

Active site5341Proton acceptor By similarity
Active site5361Cysteine radical intermediate By similarity
Active site5381Proton acceptor By similarity
Binding site3031Substrate By similarity
Binding site3471Substrate; via amide nitrogen By similarity
Site3191Important for hydrogen atom transfer By similarity
Site3261Allosteric effector binding By similarity
Site3561Allosteric effector binding By similarity
Site5741Important for hydrogen atom transfer By similarity
Site8281Important for electron transfer By similarity
Site8291Important for electron transfer By similarity
Site8401Interacts with thioredoxin/glutaredoxin By similarity
Site8431Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond319 ↔ 574Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O83972 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 47DC688E4D0B356C

FASTA84595,987
        10         20         30         40         50         60 
MHIIKRNGEP QPYMREKIIV AISAAFRSVQ NPLAPEVPAI ITDLAAEVER QLFEMNRAGV 

        70         80         90        100        110        120 
PVHVEKIQDF VEKTLTKYNH SDEVKSFILY RDDRTKKRIA REQIACCFTD SSVLGVLKEI 

       130        140        150        160        170        180 
QQDFPFPEYS LDALASKFLL FKKEVTDERR SMQLLIKAAV ELTAQEAPQW ELIAARLLML 

       190        200        210        220        230        240 
DFSLALGTSL EKLNIHSFYE KITYLEEAGL YGVYIRTHYS RAEIEEAATY LECSRDKLFT 

       250        260        270        280        290        300 
YSSLDMILRR YVIRTRAHVP LETPQEMFLG IALHLAMNET QDRMQWVKRF YTVLSKLQVT 

       310        320        330        340        350        360 
VATPTLSNAR KPFHQLSSCF VDTVPDSLDG IYRSIDNFSQ VSKFGGGMGL YFGKVRAVGA 

       370        380        390        400        410        420 
PIRGFQGAAG GILRWIKLAN DTAVAVDQLG VRQGSVAVYL DVWHKDIPEF LQLRTNNGDD 

       430        440        450        460        470        480 
RMKAHDVFPA VCYPDLFWKT VRDNLGASWY LMCPHEILTV KGYALEDFYA EEWEKRYWDC 

       490        500        510        520        530        540 
VKDARISKRT IPIKELVRLV LKSVVETGTP FAFYRDHANR ANPNGHRGII YCSNLCTEIA 

       550        560        570        580        590        600 
QNMSAINLVS VKITEVDGQK VVVQTTRPGD FVVCNLASLV LSNIDLSDDK ELREVVRVAV 

       610        620        630        640        650        660 
RALDNVIDLT YYPVPYAQVT NAYYRAIGLG VSGYHHVLAQ QGIDWESDEH LAFADRIFER 

       670        680        690        700        710        720 
INRAAIEASM TIAREKGAYG CFTGSDWCTG AYFRKRGYVS EDWQRLQREV ATHGMRNGYL 

       730        740        750        760        770        780 
LAVAPTSSTS IIAGTTAGVD PIMKQYFLEE KKGMLMPRVA PSLSQKTCPL YKSAHAVEQR 

       790        800        810        820        830        840 
WSIRAAGLRQ RHIDQAQSVN LYITTDFTLK QVLDLYVYAW EVGMKSLYYV RSQSLEIDLC 


GYCAS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000520 Genomic DNA. Translation: AAC65956.1.
PIRB71255.
RefSeqNP_219445.1. NC_000919.1.
YP_008091827.1. NC_021490.2.

3D structure databases

ProteinModelPortalO83972.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO83972. 2 interactions.
STRING243276.TP1008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC65956; AAC65956; TP_1008.
GeneID15852298.
2610819.
KEGGtpa:TP1008.
tpw:TPANIC_1008.
PATRIC20532141. VBITrePal57110_1063.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMAIHPIVSR.
OrthoDBEOG6J48HC.
ProtClustDBPRK12364.

Enzyme and pathway databases

BioCycTPAL243276:GC1H-1063-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. 1 hit.
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. 1 hit.
PS00089. RIBORED_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIR1_TREPA
AccessionPrimary (citable) accession number: O83972
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: January 22, 2014
This is version 99 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