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Q00248

- PDI_ASPOR

UniProt

Q00248 - PDI_ASPOR

Protein

Protein disulfide-isomerase

Gene

pdiA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.By similarity

    Catalytic activityi

    Catalyzes the rearrangement of -S-S- bonds in proteins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei58 – 581NucleophileBy similarity
    Sitei59 – 591Contributes to redox potential valueBy similarity
    Sitei60 – 601Contributes to redox potential valueBy similarity
    Active sitei61 – 611NucleophileBy similarity
    Sitei121 – 1211Lowers pKa of C-terminal Cys of first active siteBy similarity
    Active sitei393 – 3931NucleophileBy similarity
    Sitei394 – 3941Contributes to redox potential valueBy similarity
    Sitei395 – 3951Contributes to redox potential valueBy similarity
    Active sitei396 – 3961NucleophileBy similarity
    Sitei456 – 4561Lowers pKa of C-terminal Cys of second active siteBy similarity

    GO - Molecular functioni

    1. protein disulfide isomerase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Isomerase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein disulfide-isomerase (EC:5.3.4.1)
    Short name:
    PDI
    Gene namesi
    Name:pdiA
    ORF Names:AO090001000733
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 2

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. extracellular region Source: ASPGD

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 515495Protein disulfide-isomerasePRO_0000034214Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 61Redox-activePROSITE-ProRule annotation
    Disulfide bondi393 ↔ 396Redox-activePROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi5062.CADAORAP00000656.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00248.
    SMRiQ00248. Positions 235-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 136116Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini343 – 470128Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi512 – 5154Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the protein disulfide isomerase family.Curated
    Contains 2 thioredoxin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000162459.
    KOiK09580.
    OMAiPYSGARK.
    OrthoDBiEOG71CFZN.

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PfamiPF00085. Thioredoxin. 2 hits.
    [Graphical view]
    SUPFAMiSSF52833. SSF52833. 4 hits.
    TIGRFAMsiTIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q00248-1 [UniParc]FASTAAdd to Basket

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    MRTFAPWILS LLGASAVASA ADATAEAPSD VVSLTGDTFE TFVKEHDLVL    50
    AEFFAPWCGH CKALAPKYEQ AATELKEKNI PLVKVDCTEE EALCRDQGVE 100
    GYPTLKIFRG LDAVKPYQGA RQTEAIVSYM VKQSLPAVSP VTPENLEEIK 150
    TMDKIVVIGY IASDDQTAND IFTTFAESQR DNYLFAATSD ASIAKAEGVK 200
    QPSIVLYKDF DEKKATYDGE IEQDALLSWV KTASTPLVGE LGPETYSGYI 250
    TAGIPLAYIF AETKEEREQF TEEFKFIAEK HKGSINIVTI DAKLYGAHAG 300
    NLNLDPSKFP AFAIQDPEKN AKYPYDQSKE VKAKDIGKFI QDVLDDKVEP 350
    SIKSEAIPET QEGPVTVVVA HSYKDLVLDN EKDVLLEFYA PWCGHCKALA 400
    PKYEELASLY KDIPEVTIAK IDATANDVPD SITGFPTIKL FAAGAKDSPV 450
    EYEGSRTVED LANFVKENGK HKVDALEVDP KKEQESGDAT ETRAASDETE 500
    TPAATSDDKS EHDEL 515
    Length:515
    Mass (Da):56,458
    Last modified:November 1, 1997 - v1
    Checksum:iA155B38E20E37EAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85900 Genomic DNA. Translation: BAA12913.1.
    AP007154 Genomic DNA. Translation: BAE57222.1.
    RefSeqiXP_001819224.1. XM_001819172.2.

    Genome annotation databases

    EnsemblFungiiCADAORAT00000669; CADAORAP00000656; CADAORAG00000669.
    GeneIDi5991195.
    KEGGiaor:AOR_1_1320164.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85900 Genomic DNA. Translation: BAA12913.1 .
    AP007154 Genomic DNA. Translation: BAE57222.1 .
    RefSeqi XP_001819224.1. XM_001819172.2.

    3D structure databases

    ProteinModelPortali Q00248.
    SMRi Q00248. Positions 235-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5062.CADAORAP00000656.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00000669 ; CADAORAP00000656 ; CADAORAG00000669 .
    GeneIDi 5991195.
    KEGGi aor:AOR_1_1320164.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000162459.
    KOi K09580.
    OMAi PYSGARK.
    OrthoDBi EOG71CFZN.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR005788. Disulphide_isomerase.
    IPR005792. Prot_disulphide_isomerase.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00085. Thioredoxin. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52833. SSF52833. 4 hits.
    TIGRFAMsi TIGR01130. ER_PDI_fam. 1 hit.
    TIGR01126. pdi_dom. 2 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization and overexpression of a gene (pdiA) encoding protein disulfide isomerase of Aspergillus oryzae."
      Lee B., Yamada O., Kitamoto K., Takahashi K.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.
    2. "Genome sequencing and analysis of Aspergillus oryzae."
      Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
      , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
      Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 42149 / RIB 40.

    Entry informationi

    Entry nameiPDI_ASPOR
    AccessioniPrimary (citable) accession number: Q00248
    Secondary accession number(s): Q2UMJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3