PDI_ASPOR
ID PDI_ASPOR Reviewed; 515 AA.
AC Q00248; Q2UMJ3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Protein disulfide-isomerase;
DE Short=PDI;
DE EC=5.3.4.1;
DE Flags: Precursor;
GN Name=pdiA; ORFNames=AO090001000733;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RA Lee B., Yamada O., Kitamoto K., Takahashi K.;
RT "Cloning, characterization and overexpression of a gene (pdiA) encoding
RT protein disulfide isomerase of Aspergillus oryzae.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC bonds, may be involved in glycosylation, prolyl hydroxylation and
CC triglyceride transfer. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000305}.
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DR EMBL; D85900; BAA12913.1; -; Genomic_DNA.
DR EMBL; AP007154; BAE57222.1; -; Genomic_DNA.
DR RefSeq; XP_001819224.1; XM_001819172.2.
DR AlphaFoldDB; Q00248; -.
DR SMR; Q00248; -.
DR STRING; 510516.Q00248; -.
DR EnsemblFungi; BAE57222; BAE57222; AO090001000733.
DR GeneID; 5991195; -.
DR KEGG; aor:AO090001000733; -.
DR VEuPathDB; FungiDB:AO090001000733; -.
DR HOGENOM; CLU_025879_5_0_1; -.
DR OMA; YIAKHAT; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 4.
DR TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Isomerase; Redox-active center;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..515
FT /note="Protein disulfide-isomerase"
FT /id="PRO_0000034214"
FT DOMAIN 21..136
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 343..470
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 472..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 512..515
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 472..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 121
FT /note="Lowers pKa of C-terminal Cys of first active site"
FT /evidence="ECO:0000250"
FT SITE 394
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 395
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 456
FT /note="Lowers pKa of C-terminal Cys of second active site"
FT /evidence="ECO:0000250"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 393..396
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 515 AA; 56458 MW; A155B38E20E37EAC CRC64;
MRTFAPWILS LLGASAVASA ADATAEAPSD VVSLTGDTFE TFVKEHDLVL AEFFAPWCGH
CKALAPKYEQ AATELKEKNI PLVKVDCTEE EALCRDQGVE GYPTLKIFRG LDAVKPYQGA
RQTEAIVSYM VKQSLPAVSP VTPENLEEIK TMDKIVVIGY IASDDQTAND IFTTFAESQR
DNYLFAATSD ASIAKAEGVK QPSIVLYKDF DEKKATYDGE IEQDALLSWV KTASTPLVGE
LGPETYSGYI TAGIPLAYIF AETKEEREQF TEEFKFIAEK HKGSINIVTI DAKLYGAHAG
NLNLDPSKFP AFAIQDPEKN AKYPYDQSKE VKAKDIGKFI QDVLDDKVEP SIKSEAIPET
QEGPVTVVVA HSYKDLVLDN EKDVLLEFYA PWCGHCKALA PKYEELASLY KDIPEVTIAK
IDATANDVPD SITGFPTIKL FAAGAKDSPV EYEGSRTVED LANFVKENGK HKVDALEVDP
KKEQESGDAT ETRAASDETE TPAATSDDKS EHDEL
