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Q00248

- PDI_ASPOR

UniProt

Q00248 - PDI_ASPOR

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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: 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)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
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
ProteomesiUP000006564: Chromosome 2

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular region Source: ASPGD
Complete GO annotation...

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 [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:
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

« Hide 'large scale' publications
  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 29, 2014
This is version 102 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