DB code: D00870
| RLCP classification | 3.676.249900.37 : Transfer | |
|---|---|---|
| CATH domain | 3.40.30.10 : Glutaredoxin | Catalytic domain |
| 3.30.1020.10 : Antioxidant, Horf6; Chain A, domain 2 | ||
| E.C. | 1.11.1.15 | |
| CSA | ||
| M-CSA | ||
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.30.10 : Glutaredoxin | S00916 S00279 M00184 D00866 D00869 D00278 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| Q86SB3 |
|
1-Cys peroxiredoxin
|
PF10417
(1-cysPrx_C)
PF00578 (AhpC-TSA) [Graphical View] |
| KEGG enzyme name |
|---|
|
Peroxiredoxin
Thioredoxin peroxidase Tryparedoxin peroxidase Alkyl hydroperoxide reductase C22 AhpC TrxPx TXNPx Prx PRDX |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| Q86SB3 | Q86SB3_9APIC |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C16736 | C15498 | C15496 | C00001 | C01335 | I00142 | I00143 | |||||
| E.C. | ||||||||||||
| Compound | R'-SH | ROOH | R-S-S-R | H2O | ROH | Peptidyl-Cys-sulfenic acid | Transient disulfide bond between peptidyl-Cys | |||||
| Type | sulfhydryl group | others | disulfide bond | H2O | carbohydrate | |||||||
| ChEBI |
15377 15377 |
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| PubChem |
22247451 962 22247451 962 |
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| 1xccA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xccB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xccC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xccD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3tb2A01 |
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Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CSD | Unbound | |
| 3tb2B01 |
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Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CSD | Unbound | |
| 3tb2C01 |
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Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CSD | Unbound | |
| 3tb2D01 |
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Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CSD | Unbound | |
| 1xccA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xccB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xccC02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1xccD02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3tb2A02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3tb2B02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3tb2C02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3tb2D02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Literature [1], [2], [4], [5], [6] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1xccA01 |
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THR 44;CYS 47;ARG 129 | ASN 41;VAL 46;CYS 47 | |||
| 1xccB01 |
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THR 44;CYS 47;ARG 129 | ASN 41;VAL 46;CYS 47 | |||
| 1xccC01 |
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THR 44;CYS 47;ARG 129 | ASN 41;VAL 46;CYS 47 | |||
| 1xccD01 |
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THR 44;CYS 47;ARG 129 | ASN 41;VAL 46;CYS 47 | |||
| 3tb2A01 |
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THR 44; ;ARG 129 | CSD 47(3-Sulfinoalanine) | ASN 41;VAL 46;CYS 47 | ||
| 3tb2B01 |
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THR 44; ;ARG 129 | CSD 47(3-Sulfinoalanine) | ASN 41;VAL 46;CYS 47 | ||
| 3tb2C01 |
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THR 44; ;ARG 129 | CSD 47(3-Sulfinoalanine) | ASN 41;VAL 46;CYS 47 | ||
| 3tb2D01 |
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THR 44; ;ARG 129 | CSD 47(3-Sulfinoalanine) | ASN 41;VAL 46;CYS 47 | ||
| 1xccA02 |
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| 1xccB02 |
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| 1xccC02 |
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| 1xccD02 |
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| 3tb2A02 |
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| 3tb2B02 |
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| 3tb2C02 |
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| 3tb2D02 |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
|
Fig. 4 | |
|
[2]
|
Fig. 1 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
| Medline ID | |
| PubMed ID | 9587003 |
| Journal | Nat Struct Biol |
| Year | 1998 |
| Volume | 5 |
| Pages | 400-6 |
| Authors | Choi HJ, Kang SW, Yang CH, Rhee SG, Ryu SE |
| Title | Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. |
| Related PDB | 1prx |
| Related UniProtKB | P30041 |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12517450 |
| Journal | Trends Biochem Sci |
| Year | 2003 |
| Volume | 28 |
| Pages | 32-40 |
| Authors | Wood ZA, Schroder E, Robin Harris J, Poole LB |
| Title |
Structure, |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), |
| Medline ID | |
| PubMed ID | 17125854 |
| Journal | Mol Biochem Parasitol |
| Year | 2007 |
| Volume | 151 |
| Pages | 100-10 |
| Authors | Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R |
| Title | Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. |
| Related PDB | 1xcc 3tb2 |
| Related UniProtKB | Q86SB3 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 18084889 |
| Journal | Subcell Biochem |
| Year | 2007 |
| Volume | 44 |
| Pages | 41-60 |
| Authors | Karplus PA, Hall A |
| Title | Structural survey of the peroxiredoxins. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 20969484 |
| Journal | Antioxid Redox Signal |
| Year | 2011 |
| Volume | 15 |
| Pages | 795-815 |
| Authors | Hall A, Nelson K, Poole LB, Karplus PA |
| Title | Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 22429898 |
| Journal | BMC Struct Biol |
| Year | 2012 |
| Volume | 12 |
| Pages | 2 |
| Authors | Qiu W, Dong A, Pizarro JC, Botchkarsev A, Min J, Wernimont AK, Hills T, Hui R, Artz JD |
| Title | Crystal structures from the Plasmodium peroxiredoxins: new insights into oligomerization and product binding. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
Peroxiredoxins (Prxs) can be classified into three categories (see [2]):
(1) typical 2-Cys Prxs; conservation of two redox-active cysteines; homodimers having two identical active sites. (2) atypical 2-Cys Prxs; conservation of two redox-active cysteines; functionally monomeric. (3) 1-Cys Prxs; only one cysteine. This enzyme belongs to the category of 1-Cys Prxs. The redox-active cysteine is referred to as the peroxidatic cysteine, Since this enzyme is homologous to 1-Cys Prxs (D00869, Thus, (A) Transfer of peroxide oxygen from another peroxide oxygen to the perdoxidatic Cys, (B) Transfer of sulfur atom of the peroxidatic Cys from the hydroxyl group to thiol (or sulfhydryl) group of the second substrat (C) Electron transfer from thiol of the third substrate (or another R'-SH) to the disulfide bond (thiol-disulfide exchange): Although this enzyme can be over-oxidized to form sulfinic acid (-SO2H) and further oxidized sulfonic acid (-SO3H), |
| Created | Updated |
|---|---|
| 2012-07-12 | 2012-09-13 |