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
PubChem 22247451
962
1xccA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xccB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xccC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xccD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3tb2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Intermediate-analogue:CSD Unbound
3tb2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Intermediate-analogue:CSD Unbound
3tb2C01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Intermediate-analogue:CSD Unbound
3tb2D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Intermediate-analogue:CSD Unbound
1xccA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xccB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xccC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1xccD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3tb2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3tb2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3tb2C02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
3tb2D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44;CYS 47;ARG 129 ASN 41;VAL 46;CYS 47
1xccB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44;CYS 47;ARG 129 ASN 41;VAL 46;CYS 47
1xccC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44;CYS 47;ARG 129 ASN 41;VAL 46;CYS 47
1xccD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44;CYS 47;ARG 129 ASN 41;VAL 46;CYS 47
3tb2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44; ;ARG 129 CSD 47(3-Sulfinoalanine) ASN 41;VAL 46;CYS 47
3tb2B01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44; ;ARG 129 CSD 47(3-Sulfinoalanine) ASN 41;VAL 46;CYS 47
3tb2C01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44; ;ARG 129 CSD 47(3-Sulfinoalanine) ASN 41;VAL 46;CYS 47
3tb2D01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain THR 44; ;ARG 129 CSD 47(3-Sulfinoalanine) ASN 41;VAL 46;CYS 47
1xccA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1xccB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1xccC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1xccD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tb2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tb2B02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tb2C02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3tb2D02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

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, mechanism and regulation of peroxiredoxins.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SULFINATION AT CYS-47.
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, in contrast to the second cysteine, the resolving cysteine, in the 2-Cys Prxs.
Since this enzyme is homologous to 1-Cys Prxs (D00869, S00916 in EzCatDB) with a similar active site, it must have a similar catalytic mechanism as the homologue.
Thus, this enzyme catalyzes the following reactions (see [2]):
(A) Transfer of peroxide oxygen from another peroxide oxygen to the perdoxidatic Cys, forming Cys-sulfenic acid:
(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), over-oxidization mechanism is not described in this entry. Incidentally, 3tb2 (of PDB) gives structures of sulfinic acid form.

Created Updated
2012-07-12 2012-09-13