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P43754

- RIR1_HAEIN

UniProt

P43754 - RIR1_HAEIN

Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdA

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Enzyme regulationi

    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.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91Allosteric activatorBy similarity
    Binding sitei55 – 551Allosteric activatorBy similarity
    Binding sitei91 – 911Allosteric activatorBy similarity
    Binding sitei209 – 2091SubstrateBy similarity
    Sitei225 – 2251Important for hydrogen atom transferBy similarity
    Sitei232 – 2321Allosteric effector bindingBy similarity
    Binding sitei253 – 2531Substrate; via amide nitrogenBy similarity
    Sitei262 – 2621Allosteric effector bindingBy similarity
    Active sitei437 – 4371Proton acceptorBy similarity
    Active sitei439 – 4391Cysteine radical intermediateBy similarity
    Active sitei441 – 4411Proton acceptorBy similarity
    Sitei462 – 4621Important for hydrogen atom transferBy similarity
    Sitei730 – 7301Important for electron transferBy similarity
    Sitei731 – 7311Important for electron transferBy similarity
    Sitei749 – 7491Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei754 – 7541Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB-EC

    GO - Biological processi

    1. DNA replication Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit alpha (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleotide reductase
    Gene namesi
    Name:nrdA
    Ordered Locus Names:HI_1659
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 756756Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi225 ↔ 462Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP43754.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi71421.HI1659.

    Structurei

    3D structure databases

    ProteinModelPortaliP43754.
    SMRiP43754. Positions 5-737.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9591ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 217Allosteric activator bindingBy similarity
    Regioni224 – 2252Substrate bindingBy similarity
    Regioni437 – 4415Substrate bindingBy similarity
    Regioni621 – 6255Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    KOiK00525.
    OMAiLLWQMPS.
    OrthoDBiEOG6J48HC.
    PhylomeDBiP43754.

    Family and domain databases

    InterProiIPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P43754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKSLMVTKR DGTQEQINLD KIHRVITWAA EGLDNVSVSQ VELRSHIQFY    50
    EGIRTSDIHE TIIKAAADLI SKDSPDYQYL AARLAIFHLR KKAYGHFDPP 100
    RLYDHVKKLV RMEKYDQALL DDYTREEWDT MDGFIDHWRD MTFSYAAVKQ 150
    LEGKYLVQNR VTGEIYESAQ FLYLLVSASL FSKYPKETRL DYVKRFYDAT 200
    STFKISLPTP IMAGVRTPTR QFSSCVLIEC DDSLDSINAT ASAIVKYVSQ 250
    RAGIGINAGA IRALGSEIRG GEAFHTGCIP FYKYFQTAVK SCSQGGVRGG 300
    AATLYYPIWH LEAENLLVLK NNRGVEDNRV RHMDYGVQLN KLMYQRLIKG 350
    SEITLFSPSD VPGLYEAFFA DQDKFEELYV KYEQDPTIRK RTVKAVEIFS 400
    LLMQERASTG RIYIQNVDHC NTHSPFDPQV APVRQSNLCL EIALPTKPLQ 450
    HINDENGEIA LCTLSAFNLG KIENLDELEE LADLAVRSLD ALLDYQDYPV 500
    VAAKRSSLAR RSLGIGVINY AYYLAKNGVR YSDGSANDLT HRTFEAIQYY 550
    LLKASMNLAK EQGACEYFNE TTYAKGILPI DTYKKDLDSL TQEPLHYDWE 600
    SLRKDIQEFG LRNSTLTALM PSETSSQISN ATNGIEPPRG HVSIKASKDG 650
    ILKQVVPEYE NLMDNYELLW DIPSNDGYLH LVGIMQKFVD QAISANTNYD 700
    PKRFEDGKVP MKVLLKDLLT AYKYGLKTLY YQNTRDGAED VQEDLDDGCA 750
    GGACKI 756
    Length:756
    Mass (Da):85,696
    Last modified:November 1, 1995 - v1
    Checksum:i839D02FA61E185D3
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23305.1. Different initiation.
    PIRiB64135.
    RefSeqiNP_439801.2. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC23305; AAC23305; HI_1659.
    GeneIDi950495.
    KEGGihin:HI1659.
    PATRICi20192067. VBIHaeInf48452_1737.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC23305.1 . Different initiation.
    PIRi B64135.
    RefSeqi NP_439801.2. NC_000907.1.

    3D structure databases

    ProteinModelPortali P43754.
    SMRi P43754. Positions 5-737.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI1659.

    Proteomic databases

    PRIDEi P43754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC23305 ; AAC23305 ; HI_1659 .
    GeneIDi 950495.
    KEGGi hin:HI1659.
    PATRICi 20192067. VBIHaeInf48452_1737.

    Phylogenomic databases

    eggNOGi COG0209.
    KOi K00525.
    OMAi LLWQMPS.
    OrthoDBi EOG6J48HC.
    PhylomeDBi P43754.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Family and domain databases

    InterProi IPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiRIR1_HAEIN
    AccessioniPrimary (citable) accession number: P43754
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3