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Q9PL93

- RIR1_CHLMU

UniProt

Q9PL93 - RIR1_CHLMU

Protein

Ribonucleoside-diphosphate reductase subunit alpha

Gene

nrdA

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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. 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.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei442 – 4421SubstrateBy similarity
    Sitei458 – 4581Important for hydrogen atom transferBy similarity
    Sitei465 – 4651Allosteric effector bindingBy similarity
    Binding sitei486 – 4861Substrate; via amide nitrogenBy similarity
    Sitei495 – 4951Allosteric effector bindingBy similarity
    Active sitei670 – 6701Proton acceptorBy similarity
    Active sitei672 – 6721Cysteine radical intermediateBy similarity
    Active sitei674 – 6741Proton acceptorBy similarity
    Sitei687 – 6871Important for hydrogen atom transferBy similarity
    Sitei990 – 9901Important for electron transferBy similarity
    Sitei991 – 9911Important for electron transferBy similarity
    Sitei1043 – 10431Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei1046 – 10461Interacts 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

    BioCyciCMUR243161:GHYU-225-MONOMER.
    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:TC_0214
    OrganismiChlamydia muridarum (strain MoPn / Nigg)
    Taxonomic identifieri243161 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000800: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. ribonucleoside-diphosphate reductase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10471047Ribonucleoside-diphosphate reductase subunit alphaPRO_0000187210Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi458 ↔ 687Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    STRINGi243161.TC0214.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PL93.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 111103ATP-cone 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini118 – 219102ATP-cone 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 32791ATP-cone 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni457 – 4582Substrate bindingBy similarity
    Regioni670 – 6745Substrate bindingBy similarity
    Regioni857 – 8615Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 3 ATP-cone domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0209.
    KOiK00525.
    OMAiANGSIQH.
    OrthoDBiEOG6J48HC.

    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. 2 hits.
    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. 3 hits.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9PL93-1 [UniParc]FASTAAdd to Basket

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    MVDLQEKQCT IVKRNGMFVP FDRNRIFQAL EAAFRDTRRI DDHMPLPEDL     50
    ENSIRSITHQ VVKEVVQKIT DGQVVTVERI QDMVESQLYI NGLQDVARDY 100
    VVYRDDRKAH REKSWQSLSV IRRCGTTVHF NPMKISAALE KAFRATDRIE 150
    GMTPDFVREE VNALTQKIVA EIEERCSQQD SRIDIEQIQD IVEQQLMVVG 200
    HYATAKNYIL YREARARVRD NRVEDQIVEE APSEETFEVL SKDGSTYMIT 250
    HSQLLARLAR ACSRFPETTD AALLTDMAFS NFYSGIKESE VVLACIMAAR 300
    ANIEKEPDYA FVAAELLLDV VYKEALDRSR GDEDLEQVYR DHFKRYIMEG 350
    DSYRLNPELK NLFDLDALAN AMDLSRDLQF SYMGIQNLYD RYFNHDDGRR 400
    LETPQIFWMR VAMGLALKEQ DKTYWAITFY NLLSTFRYTP ATPTLFNSGM 450
    RHSQLSSCYL STVQDDLVNI YKVISDNAML SKWAGGIGND WTAIRATGAL 500
    IKGTNGKSQG VIPFIKVTND TAVAVNQGGK RKGAVCVYLE VWHLDYEDFL 550
    ELRKNTGDDR RRAHDVNTAS WIPDLFFKRL QQKGSWTLFS PDDVPGLHDA 600
    YGEEFERLYE EYERKVDSGE IRLYKKVEAE DLWRKMLSML FETGHPWMTF 650
    KDPSNIRSAQ DHTGVVRCSN LCTEILLNCS ETETAVCNLG SVNLVQHILD 700
    DGLDEEKLSE TISIAVRMLD NVIDINFYPT KEAKEANFAH RAIGLGVMGF 750
    QDALYKLDIS YASQEAVEFA DYSSELISYY AIQASCLLAK ERGTYSSYKG 800
    SKWDRGLLPI DTIQLLANYR GKDNLQMDTS VRKDWEPIRS LIREHGMRNC 850
    QLMAIAPTAT ISNIIGVTQS IEPTYKHLFV KSNLSGEFTI PNVYLIEKLK 900
    KLGIWDADML DDLKYFDGSL LEIERVPDHI KHIFLTAFEI EPEWILECAS 950
    RRQKWIDMGQ SLNLYLAQPD GKKLSNMYLT AWKKGLKTTY YLRSSSATTV 1000
    EKSFVDINKR GIQPRWMKNK SASAGIVVER ASKTPVCSLE EGCEVCQ 1047
    Length:1,047
    Mass (Da):120,036
    Last modified:October 1, 2000 - v1
    Checksum:i9B3FFD9BFAF817AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39086.1.
    PIRiF81728.
    RefSeqiNP_296593.1. NC_002620.2.

    Genome annotation databases

    EnsemblBacteriaiAAF39086; AAF39086; TC_0214.
    GeneIDi1246340.
    KEGGicmu:TC_0214.
    PATRICi20371810. VBIChlMur19118_0234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39086.1 .
    PIRi F81728.
    RefSeqi NP_296593.1. NC_002620.2.

    3D structure databases

    ProteinModelPortali Q9PL93.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243161.TC0214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF39086 ; AAF39086 ; TC_0214 .
    GeneIDi 1246340.
    KEGGi cmu:TC_0214.
    PATRICi 20371810. VBIChlMur19118_0234.

    Phylogenomic databases

    eggNOGi COG0209.
    KOi K00525.
    OMAi ANGSIQH.
    OrthoDBi EOG6J48HC.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .
    BioCyci CMUR243161:GHYU-225-MONOMER.

    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. 2 hits.
    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. 3 hits.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MoPn / Nigg.

    Entry informationi

    Entry nameiRIR1_CHLMU
    AccessioniPrimary (citable) accession number: Q9PL93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 97 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3