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Protein

Protein disulfide-isomerase

Gene

pdiA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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)DescriptionActionsGraphical viewLength
Active sitei58NucleophileBy similarity1
Sitei59Contributes to redox potential valueBy similarity1
Sitei60Contributes to redox potential valueBy similarity1
Active sitei61NucleophileBy similarity1
Sitei121Lowers pKa of C-terminal Cys of first active siteBy similarity1
Active sitei393NucleophileBy similarity1
Sitei394Contributes to redox potential valueBy similarity1
Sitei395Contributes to redox potential valueBy similarity1
Active sitei396NucleophileBy similarity1
Sitei456Lowers pKa of C-terminal Cys of second active siteBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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
Proteomesi
  • UP000006564 Componenti: Chromosome 2

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000003421421 – 515Protein disulfide-isomeraseAdd BLAST495

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 61Redox-activePROSITE-ProRule annotation
Disulfide bondi393 ↔ 396Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ00248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 136Thioredoxin 1PROSITE-ProRule annotationAdd BLAST116
Domaini343 – 470Thioredoxin 2PROSITE-ProRule annotationAdd BLAST128

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi512 – 515Prevents secretion from ERPROSITE-ProRule annotation4

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

HOGENOMiHOG000162459.
KOiK09580.
OMAiTSYMVKQ.
OrthoDBiEOG092C3SRA.

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

« Hide

        10         20         30         40         50
MRTFAPWILS LLGASAVASA ADATAEAPSD VVSLTGDTFE TFVKEHDLVL
60 70 80 90 100
AEFFAPWCGH CKALAPKYEQ AATELKEKNI PLVKVDCTEE EALCRDQGVE
110 120 130 140 150
GYPTLKIFRG LDAVKPYQGA RQTEAIVSYM VKQSLPAVSP VTPENLEEIK
160 170 180 190 200
TMDKIVVIGY IASDDQTAND IFTTFAESQR DNYLFAATSD ASIAKAEGVK
210 220 230 240 250
QPSIVLYKDF DEKKATYDGE IEQDALLSWV KTASTPLVGE LGPETYSGYI
260 270 280 290 300
TAGIPLAYIF AETKEEREQF TEEFKFIAEK HKGSINIVTI DAKLYGAHAG
310 320 330 340 350
NLNLDPSKFP AFAIQDPEKN AKYPYDQSKE VKAKDIGKFI QDVLDDKVEP
360 370 380 390 400
SIKSEAIPET QEGPVTVVVA HSYKDLVLDN EKDVLLEFYA PWCGHCKALA
410 420 430 440 450
PKYEELASLY KDIPEVTIAK IDATANDVPD SITGFPTIKL FAAGAKDSPV
460 470 480 490 500
EYEGSRTVED LANFVKENGK HKVDALEVDP KKEQESGDAT ETRAASDETE
510
TPAATSDDKS EHDEL
Length:515
Mass (Da):56,458
Last modified:November 1, 1997 - v1
Checksum:iA155B38E20E37EAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85900 Genomic DNA. Translation: BAA12913.1.
AP007154 Genomic DNA. Translation: BAE57222.1.
RefSeqiXP_001819224.1. XM_001819172.2.

Genome annotation databases

EnsemblFungiiBAE57222; BAE57222; AO090001000733.
GeneIDi5991195.
KEGGiaor:AOR_1_1320164.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85900 Genomic DNA. Translation: BAA12913.1.
AP007154 Genomic DNA. Translation: BAE57222.1.
RefSeqiXP_001819224.1. XM_001819172.2.

3D structure databases

ProteinModelPortaliQ00248.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE57222; BAE57222; AO090001000733.
GeneIDi5991195.
KEGGiaor:AOR_1_1320164.

Phylogenomic databases

HOGENOMiHOG000162459.
KOiK09580.
OMAiTSYMVKQ.
OrthoDBiEOG092C3SRA.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.