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P43754 (RIR1_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HI_1659
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length756 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 to separate specificity and activation sites on the alpha subunit. 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. Stimulated by ATP and inhibited by dATP binding to the activity site 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.

Sequence caution

The sequence AAC23305.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756Ribonucleoside-diphosphate reductase subunit alpha
PRO_0000187214

Regions

Domain5 – 9591ATP-cone
Region15 – 217Allosteric activator binding By similarity
Region224 – 2252Substrate binding By similarity
Region437 – 4415Substrate binding By similarity
Region621 – 6255Substrate binding By similarity

Sites

Active site4371Proton acceptor By similarity
Active site4391Cysteine radical intermediate By similarity
Active site4411Proton acceptor By similarity
Binding site91Allosteric activator By similarity
Binding site551Allosteric activator By similarity
Binding site911Allosteric activator By similarity
Binding site2091Substrate By similarity
Binding site2531Substrate; via amide nitrogen By similarity
Site2251Important for hydrogen atom transfer By similarity
Site2321Allosteric effector binding By similarity
Site2621Allosteric effector binding By similarity
Site4621Important for hydrogen atom transfer By similarity
Site7301Important for electron transfer By similarity
Site7311Important for electron transfer By similarity
Site7491Interacts with thioredoxin/glutaredoxin By similarity
Site7541Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond225 ↔ 462Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P43754 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 839D02FA61E185D3

FASTA75685,696
        10         20         30         40         50         60 
MNKSLMVTKR DGTQEQINLD KIHRVITWAA EGLDNVSVSQ VELRSHIQFY EGIRTSDIHE 

        70         80         90        100        110        120 
TIIKAAADLI SKDSPDYQYL AARLAIFHLR KKAYGHFDPP RLYDHVKKLV RMEKYDQALL 

       130        140        150        160        170        180 
DDYTREEWDT MDGFIDHWRD MTFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYLLVSASL 

       190        200        210        220        230        240 
FSKYPKETRL DYVKRFYDAT STFKISLPTP IMAGVRTPTR QFSSCVLIEC DDSLDSINAT 

       250        260        270        280        290        300 
ASAIVKYVSQ RAGIGINAGA IRALGSEIRG GEAFHTGCIP FYKYFQTAVK SCSQGGVRGG 

       310        320        330        340        350        360 
AATLYYPIWH LEAENLLVLK NNRGVEDNRV RHMDYGVQLN KLMYQRLIKG SEITLFSPSD 

       370        380        390        400        410        420 
VPGLYEAFFA DQDKFEELYV KYEQDPTIRK RTVKAVEIFS LLMQERASTG RIYIQNVDHC 

       430        440        450        460        470        480 
NTHSPFDPQV APVRQSNLCL EIALPTKPLQ HINDENGEIA LCTLSAFNLG KIENLDELEE 

       490        500        510        520        530        540 
LADLAVRSLD ALLDYQDYPV VAAKRSSLAR RSLGIGVINY AYYLAKNGVR YSDGSANDLT 

       550        560        570        580        590        600 
HRTFEAIQYY LLKASMNLAK EQGACEYFNE TTYAKGILPI DTYKKDLDSL TQEPLHYDWE 

       610        620        630        640        650        660 
SLRKDIQEFG LRNSTLTALM PSETSSQISN ATNGIEPPRG HVSIKASKDG ILKQVVPEYE 

       670        680        690        700        710        720 
NLMDNYELLW DIPSNDGYLH LVGIMQKFVD QAISANTNYD PKRFEDGKVP MKVLLKDLLT 

       730        740        750 
AYKYGLKTLY YQNTRDGAED VQEDLDDGCA GGACKI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC23305.1. Different initiation.
PIRB64135.
RefSeqNP_439801.2. NC_000907.1.

3D structure databases

ProteinModelPortalP43754.
SMRP43754. Positions 5-737.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI1659.

Proteomic databases

PRIDEP43754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC23305; AAC23305; HI_1659.
GeneID950495.
KEGGhin:HI1659.
PATRIC20192067. VBIHaeInf48452_1737.

Phylogenomic databases

eggNOGCOG0209.
KOK00525.
OMAKSHIQFY.
OrthoDBEOG6J48HC.
ProtClustDBPRK09103.

Enzyme and pathway databases

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_HAEIN
AccessionPrimary (citable) accession number: P43754
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 13, 2013
This is version 105 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names