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

Q00248 (PDI_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Protein disulfide-isomerase

Short name=PDI
EC=5.3.4.1
Gene names
Name:pdiA
ORF Names:AO090001000733
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Endoplasmic reticulum lumen By similarity.

Sequence similarities

Belongs to the protein disulfide isomerase family.

Contains 2 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 515495Protein disulfide-isomerase
PRO_0000034214

Regions

Domain21 – 136116Thioredoxin 1
Domain343 – 470128Thioredoxin 2
Motif512 – 5154Prevents secretion from ER Potential

Sites

Active site581Nucleophile By similarity
Active site611Nucleophile By similarity
Active site3931Nucleophile By similarity
Active site3961Nucleophile By similarity
Site591Contributes to redox potential value By similarity
Site601Contributes to redox potential value By similarity
Site1211Lowers pKa of C-terminal Cys of first active site By similarity
Site3941Contributes to redox potential value By similarity
Site3951Contributes to redox potential value By similarity
Site4561Lowers pKa of C-terminal Cys of second active site By similarity

Amino acid modifications

Disulfide bond58 ↔ 61Redox-active By similarity
Disulfide bond393 ↔ 396Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00248 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A155B38E20E37EAC

FASTA51556,458
        10         20         30         40         50         60 
MRTFAPWILS LLGASAVASA ADATAEAPSD VVSLTGDTFE TFVKEHDLVL AEFFAPWCGH 

        70         80         90        100        110        120 
CKALAPKYEQ AATELKEKNI PLVKVDCTEE EALCRDQGVE GYPTLKIFRG LDAVKPYQGA 

       130        140        150        160        170        180 
RQTEAIVSYM VKQSLPAVSP VTPENLEEIK TMDKIVVIGY IASDDQTAND IFTTFAESQR 

       190        200        210        220        230        240 
DNYLFAATSD ASIAKAEGVK QPSIVLYKDF DEKKATYDGE IEQDALLSWV KTASTPLVGE 

       250        260        270        280        290        300 
LGPETYSGYI TAGIPLAYIF AETKEEREQF TEEFKFIAEK HKGSINIVTI DAKLYGAHAG 

       310        320        330        340        350        360 
NLNLDPSKFP AFAIQDPEKN AKYPYDQSKE VKAKDIGKFI QDVLDDKVEP SIKSEAIPET 

       370        380        390        400        410        420 
QEGPVTVVVA HSYKDLVLDN EKDVLLEFYA PWCGHCKALA PKYEELASLY KDIPEVTIAK 

       430        440        450        460        470        480 
IDATANDVPD SITGFPTIKL FAAGAKDSPV EYEGSRTVED LANFVKENGK HKVDALEVDP 

       490        500        510 
KKEQESGDAT ETRAASDETE TPAATSDDKS EHDEL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85900 Genomic DNA. Translation: BAA12913.1.
AP007154 Genomic DNA. Translation: BAE57222.1.
RefSeqXP_001819224.1. XM_001819172.2.

3D structure databases

ProteinModelPortalQ00248.
SMRQ00248. Positions 235-472.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00000656.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00000669; CADAORAP00000656; CADAORAG00000669.
GeneID5991195.
KEGGaor:AOR_1_1320164.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000162459.
KOK09580.
OMAPYSGARK.
OrthoDBEOG71CFZN.

Family and domain databases

Gene3D3.40.30.10. 3 hits.
InterProIPR005788. Disulphide_isomerase.
IPR005792. Prot_disulphide_isomerase.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 2 hits.
[Graphical view]
SUPFAMSSF52833. SSF52833. 4 hits.
TIGRFAMsTIGR01130. ER_PDI_fam. 1 hit.
TIGR01126. pdi_dom. 2 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDI_ASPOR
AccessionPrimary (citable) accession number: Q00248
Secondary accession number(s): Q2UMJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families