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Information on EC 5.3.4.1 - protein disulfide-isomerase and Organism(s) Oryza sativa and UniProt Accession Q53LQ0

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EC Tree
     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.4 Transposing S-S bonds
                5.3.4.1 protein disulfide-isomerase
IUBMB Comments
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
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This record set is specific for:
Oryza sativa
UNIPROT: Q53LQ0
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Word Map
The taxonomic range for the selected organisms is: Oryza sativa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
catalyses the rearrangement of -S-S- bonds in proteins
Synonyms
fibronectin, pdi, protein disulfide isomerase, erp57, pdia3, protein disulphide isomerase, cabp1, erp44, disulfide isomerase, erp72, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
protein disulfide isomerase
-
5'-MD
-
-
-
-
58 kDa glucose regulated protein
-
-
-
-
58 kDa microsomal protein
-
-
-
-
CaBP1
-
-
-
-
CaBP2
-
-
-
-
Cellular thyroid hormone binding protein
-
-
-
-
Disulfide interchange enzyme
-
-
-
-
Disulfide isomerase ER-60
-
-
-
-
DsbA
-
-
-
-
DsbC
-
-
-
-
DsbD
-
-
-
-
endoplasmic reticulum protein EUG1
-
-
-
-
ER58
-
-
-
-
ERp-72 homolog
-
-
-
-
ERp57
-
-
-
-
ERP59
-
-
-
-
ERP60
-
-
-
-
ERp72
-
-
-
-
HIP-70
-
-
-
-
Iodothyronine 5'-monodeiodinase
-
-
-
-
P55
-
-
-
-
P58
-
-
-
-
PDIp
-
-
-
-
protein disulfide isomerase
-
Protein disulfide isomerase P5
-
-
-
-
Protein disulfide isomerase-related protein
-
-
-
-
Protein disulphide isomerase
-
-
-
-
Protein ERp-72
-
-
-
-
R-cognin
-
-
-
-
Rearrangease
-
-
-
-
Reduced ribonuclease reactivating enzyme
-
-
-
-
Retina cognin
-
-
-
-
S-S rearrangase
-
-
-
-
Thyroid hormone-binding protein
-
-
-
-
Thyroxine deiodinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Protein disulfide-isomerase
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
CAS REGISTRY NUMBER
COMMENTARY hide
37318-49-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-globulin
?
show the reaction diagram
PDIL1-1 facilitates the oxidative folding of alpha-globulin
-
-
?
additional information
?
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cultivar Kinmaze
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDIL1-1 is uniformly distributed in the lumen
Manually annotated by BRENDA team
PDIL2-3 is localized mainly on the surface of the endoplasmic reticulum
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the a and a' domains of PDIL1-1 are both functional in the oxidative folding of proglutelins
malfunction
PDIL2-3 knockdown causes aberrant accumulation of prolamins in endoplasmic reticulum-derived type-I protein bodies whereas the oxidative folding of vacuole-targeted proteins, such as proglutelins and alpha-globulin, is hardly affected. PDIL2-3 knockdown inhibits the accumulation of Cys-rich 10-kD prolamin in the core of type-I protein bodies
physiological function
PDIL2-3 does not facilitate the oxidative folding of proglutelins
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
208000
PDIL2-3, gel filtration
72397
4 * 72397, PDIL2-3, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 72397, PDIL2-3, calculated from amino acid sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cys59/62/195/198Ala
the PDIL2-3 active site mutant is evenly dispersed within the endoplasmic reticulum lumen
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Onda, Y.; Nagamine, A.; Sakurai, M.; Kumamaru, T.; Ogawa, M.; Kawagoe, Y.
Distinct roles of protein disulfide isomerase and P5 sulfhydryl oxidoreductases in multiple pathways for oxidation of structurally diverse storage proteins in rice
Plant Cell
23
210-223
2011
Oryza sativa (Q53LQ0), Oryza sativa (Q67UF5), Oryza sativa
Manually annotated by BRENDA team