Gene

KWMTBOMO00487  Validated by peptides from experiments

Pre Gene Modal

BGIBMGA012304

Annotation

1-Cys_peroxiredoxin_[Bombyx_mori]

Location

Bomo_Chr1(+):13932198-13947760      View in EpiBrowser

Full name

Peroxiredoxin-6      

Alternative Name

1-Cys peroxiredoxin
Acidic calcium-independent phospholipase A2
Antioxidant protein 2
Ciliary body glutathione peroxidase
Non-selenium glutathione peroxidase
PHGPx

Location in the cell

Cytoplasmic   Reliability : 2.106

CDS

ATGCTTTTACTTGGAAAAACTTTTCCAGACTTCTCTGCCAACACAACAGAAGGCGAAATAAATTTTCACGAGTGGCTAGGAGATAAGTGGGGTATACTGTTCTCTCACCCATCAGACTTCACCCCGGTCTGCACAACAGAATTGGCTCGGGTGCTCGTCCTTCTTCCAGAGTTTGTGAAGCGCAACACAAAAGTCATTGGCCTGTCCTGTGACAGTGTATCCTCTCACTTGGAATGGTGCAAGGACATTAAGTCTTTTGCTGGTTGCAATGAAGACGAACCATTTCCTTATCCGATAATTGAAGACGAGAAGAGAGAGTTGGCCAACAAGCTCGGCATGATTGACAATGACGAATTGGATCACAAAGGAATGCCGCTGACAGCCCGTGCAGTCTTCATTGTCGATCCGAATAAGAAGTTTAGACTGTCAATATTGTATCCGGCTACGACTGGACGTAATTTTGATGAGATTCTGCGCATACTGGACTCTCTCCAGTTGACTGATAAGGCTAAAGTGGCAACGCCGGTAGATTGGAAGGCGGGTGACGACTGCATGGTGTTGCCAACCGTGCCGGAGGACCAGATCAAAACGTGTTTCCCACAGGGTGTCAACGTTGTTCCGCTTCCGTCCGGCAAGAATTATCTGAGGAAGACTGCTTGCCCTAAAATTTGA

Protein

MLLLGKTFPDFSANTTEGEINFHEWLGDKWGILFSHPSDFTPVCTTELARVLVLLPEFVKRNTKVIGLSCDSVSSHLEWCKDIKSFAGCNEDEPFPYPIIEDEKRELANKLGMIDNDELDHKGMPLTARAVFIVDPNKKFRLSILYPATTGRNFDEILRILDSLQLTDKAKVATPVDWKAGDDCMVLPTVPEDQIKTCFPQGVNVVPLPSGKNYLRKTACPKI

Description

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis.

Catalytic Activity

[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O
a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)

Biophysicochemical Properties

25 uM for H(2)O(2)
180 uM for H(2)O(2)
22 uM for tert-butyl hydroperoxide
142 uM for tert-butyl hydroperoxide
170 uM for cumene hydroperoxide
120 uM for cumene hydroperoxide
12 uM for triphenylcarbinyl hydroperoxide
34 uM for linoleic hydroperoxide
141 uM for linolenoyl hydroperoxide
135 uM for arachidonoyl hydroperoxide
120 uM for PLCP hydroperoxide
129 uM for PACP hydroperoxide
22 uM for 5-phenyl-3-pentenyl hydroperoxide
350 uM for dipalmitoyl phosphatidylcholine (at pH 4)

Subunit

Homodimer (By similarity). Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (PubMed:15004285). Interacts with APEX1. Interacts with STH. May interact with FAM168B (By similarity). May interact with HTR2A (By similarity).
Homodimer (By similarity). Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (By similarity).

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation mediated by glutathione S-transferase Pi, followed by spontaneous reduction of the enzyme with glutathione.

Similarity

Belongs to the peroxiredoxin family. Prx6 subfamily.

Keywords

Acetylation   Antioxidant   Complete proteome   Cytoplasm   Direct protein sequencing   Hydrolase   Lipid degradation   Lipid metabolism   Lysosome   Multifunctional enzyme   Oxidoreductase   Peroxidase   Phosphoprotein   Redox-active center   Reference proteome  

Feature

chain  Peroxiredoxin-6

Uniprot

A8D0B7   Q2F6C8   A0A212EQF8   S4NJ02   A0A2H1WM86   A0A2A4J269   + More
A0A194QZI0   A0A2S0RQR9   T1TCE9   U5ET43   A0A182Y299   A0A1Y1N188   A0A1L8E456   A0A182L3E2   D6WJ53   A0A182WWP6   A0A182M6M9   Q7QIQ4   A0A182I6Y2   A0A182PF44   A0A182V5P2   A0A182TU07   A0A182QC30   A0A1B6FZH1   A0A2M4BYL2   A0A0K8TS29   A0A2M4BYQ0   A0A182R343   A0A182JXG7   A0A182FDP3   W8CC17   A0A1J1J5H9   A0A182WL43   B5G0S1   A0A218V5B1   V5GAQ6   T1DJM5   A0A084W9Y0   A0A1B6BZ20   A0A1B6KS88   A0A0C9R5D5   W5JFL0   A0A182NJL3   U3JMG6   A0A2M4AX40   A0A336LYC4   A0A336M4R2   B5G0S3   A0A3M0K533   A0A2M4AX00   A0A0K8US52   A0A026X1B2   A0A034VZ73   A0A0A1WIE6   A0A2L2Y558   A0A182IXP6   W8Q918   A0A182YTR2   F6RBB7   E2C0C6   A0A088AKM8   N6U1R2   J3JW46   A0A2H4GVH0   A0A2Y9F3L9   E0VEQ3   A0A2I0MC11   K4FY71   H9CTT2   A0A2I7NB29   A0A2U3WK92   A0A1B6HC28   W5PQA8   A0A226MRT1   A0A226PVT3   A0A341ADK1   A0A2Y9MUT0   L8IXN6   M4T8F1   A0A212CR39   O77834   A0A2U3XU27   K4G5J3   A0A340WI73   A0A383YRH6   A0A2Y9GGK9   F1NBV0   A0A2P4TBV4   F1PC59   A0A158NH13   K4G7M7   A0A2I2UL25   A0A195B6G1   M3XZW0   A0A2Y9JSS2   A0A1V4JYA8   Q5ZJF4   A0A369S9G8   B3RP43   A0A1S3F3K8  

EC Number

1.11.1.15

Pubmed

17933572    19121390    22118469    23622113    26354079    25244985    + More
28004739    20966253    18362917    19820115    12364791    14747013    17210077    26369729    24495485    17018643    24438588    20920257    23761445    24508170    30249741    25348373    25830018    26561354    24747012    24389255    15562597    18464734    20798317    23537049    22516182    20566863    23371554    23056606    29326594    20809919    24621616    22751099    25712755    9748299    10409692    16305752    2373154    9787801    15004285    15592404    16341006    21347285    17975172    15642098    30042472    18719581   

EMBL

BABH01016932    BABH01016933    BABH01016934    BABH01016935    EU128675    ABV32570.1    + More
DQ311144    ABD36089.1    AGBW02013269    OWR43730.1    GAIX01013874    JAA78686.1    ODYU01009260    SOQ53554.1    NWSH01003565    PCG66101.1    KQ461108    KPJ09001.1    MF979110    AWA45973.1    KC996761    AGT62471.1    GANO01002097    JAB57774.1    GEZM01015464    GEZM01015463    JAV91629.1    GFDF01000554    JAV13530.1    KQ971342    EFA04630.1    AXCM01003872    AAAB01008807    EAA04146.2    APCN01003711    AXCN02000440    GECZ01014184    JAS55585.1    GGFJ01008999    MBW58140.1    GDAI01000446    JAI17157.1    GGFJ01009001    MBW58142.1    GAMC01004291    JAC02265.1    CVRI01000070    CRL07210.1    DQ215156    DQ215157    DQ215159    EF191678    EF191685    ACH44882.1    MUZQ01000049    OWK60910.1    GALX01001261    JAB67205.1    GAMD01001371    JAB00220.1    ATLV01021970    KE525326    KFB47024.1    GEDC01031019    JAS06279.1    GEBQ01025664    JAT14313.1    GBYB01011519    JAG81286.1    ADMH02001540    ETN62128.1    AGTO01020768    GGFK01012045    MBW45366.1    UFQT01000285    SSX22800.1    UFQT01000393    SSX23923.1    DQ215158    ACH44884.1    QRBI01000117    RMC08302.1    GGFK01012002    MBW45323.1    GDHF01022792    GDHF01006648    JAI29522.1    JAI45666.1    KK107063    QOIP01000005    EZA61154.1    RLU22577.1    GAKP01010341    JAC48611.1    GBXI01015635    GBXI01012416    JAC98656.1    JAD01876.1    IAAA01001924    LAA03316.1    KF745893    KF745894    KZ288285    AHL44194.1    AIR96016.1    PBC29460.1    GL451770    EFN78585.1    APGK01045856    KB741039    KB632188    ENN74546.1    ERL89793.1    BT127464    AEE62426.1    KY204028    AQW41375.1    DS235093    EEB11859.1    AKCR02000021    PKK27212.1    JX052789    AFK11017.1    JQ364950    AFD04441.1    MF467270    AUR53651.1    GECU01035475    GECU01034886    JAS72231.1    JAS72820.1    AMGL01022133    MCFN01000500    OXB57991.1    AWGT02000005    OXB84226.1    JH880647    ELR59937.1    KC342239    AGH70289.1    MKHE01000014    OWK08382.1    AF080228    AF090194    AJ243848    BT020967    BC102172    JX208657    AFM86971.1    AADN05000934    PPHD01002801    POI33850.1    AAEX03005208    ADTU01015424    JX209226    AFM87540.1    AANG04002195    KQ976574    KYM80096.1    AEYP01054466    AEYP01054467    LSYS01005497    OPJ77131.1    AJ720480    NOWV01000038    RDD43480.1    DS985242    EDV27570.1   

Proteomes

UP000005204    UP000007151    UP000218220    UP000053240    UP000076408    UP000075882    + More
UP000007266    UP000076407    UP000075883    UP000007062    UP000075840    UP000075885    UP000075903    UP000075902    UP000075886    UP000075900    UP000075881    UP000069272    UP000183832    UP000075920    UP000197619    UP000030765    UP000000673    UP000075884    UP000016665    UP000269221    UP000053097    UP000279307    UP000075880    UP000242457    UP000076420    UP000002279    UP000008237    UP000005203    UP000019118    UP000030742    UP000248484    UP000009046    UP000053872    UP000245340    UP000002356    UP000198323    UP000198419    UP000252040    UP000248483    UP000009136    UP000245341    UP000265300    UP000261681    UP000248481    UP000000539    UP000002254    UP000005205    UP000011712    UP000078540    UP000000715    UP000248482    UP000190648    UP000253843    UP000009022    UP000081671   

PRIDE

A8D0B7    Q2F6C8    O77834    F1PC59    Q5ZJF4   

Pfam

PF10417   1-cysPrx_C        + More
PF00578   AhpC-TSA

Interpro

IPR036249   Thioredoxin-like_sf        + More
IPR024706   Peroxiredoxin_AhpC-typ       
IPR000866   AhpC/TSA       
IPR019479   Peroxiredoxin_C       
IPR013766   Thioredoxin_domain       

SUPFAM

SSF52833   SSF52833       

ProteinModelPortal

A8D0B7   Q2F6C8   A0A212EQF8   S4NJ02   A0A2H1WM86   A0A2A4J269   + More
A0A194QZI0   A0A2S0RQR9   T1TCE9   U5ET43   A0A182Y299   A0A1Y1N188   A0A1L8E456   A0A182L3E2   D6WJ53   A0A182WWP6   A0A182M6M9   Q7QIQ4   A0A182I6Y2   A0A182PF44   A0A182V5P2   A0A182TU07   A0A182QC30   A0A1B6FZH1   A0A2M4BYL2   A0A0K8TS29   A0A2M4BYQ0   A0A182R343   A0A182JXG7   A0A182FDP3   W8CC17   A0A1J1J5H9   A0A182WL43   B5G0S1   A0A218V5B1   V5GAQ6   T1DJM5   A0A084W9Y0   A0A1B6BZ20   A0A1B6KS88   A0A0C9R5D5   W5JFL0   A0A182NJL3   U3JMG6   A0A2M4AX40   A0A336LYC4   A0A336M4R2   B5G0S3   A0A3M0K533   A0A2M4AX00   A0A0K8US52   A0A026X1B2   A0A034VZ73   A0A0A1WIE6   A0A2L2Y558   A0A182IXP6   W8Q918   A0A182YTR2   F6RBB7   E2C0C6   A0A088AKM8   N6U1R2   J3JW46   A0A2H4GVH0   A0A2Y9F3L9   E0VEQ3   A0A2I0MC11   K4FY71   H9CTT2   A0A2I7NB29   A0A2U3WK92   A0A1B6HC28   W5PQA8   A0A226MRT1   A0A226PVT3   A0A341ADK1   A0A2Y9MUT0   L8IXN6   M4T8F1   A0A212CR39   O77834   A0A2U3XU27   K4G5J3   A0A340WI73   A0A383YRH6   A0A2Y9GGK9   F1NBV0   A0A2P4TBV4   F1PC59   A0A158NH13   K4G7M7   A0A2I2UL25   A0A195B6G1   M3XZW0   A0A2Y9JSS2   A0A1V4JYA8   Q5ZJF4   A0A369S9G8   B3RP43   A0A1S3F3K8  

PDB

1PRX     E-value=1.47921e-75,     Score=716

KEGG

692792    K11188 peroxiredoxin 6, 1-Cys peroxiredoxin [EC:1.11.1.7 1.11.1.15 3.1.1.-] | (RefSeq) glutathione p

PATHWAY

01100    Metabolic pathways - Bombyx mori (domestic silkworm)

GO

GO:0005623   GO:0051920   GO:0045454   GO:0004601   GO:0034599   GO:0005829   GO:0042744   GO:0048471   GO:0042803   GO:0046475   GO:0006979   GO:0004602   GO:0048026   GO:0031625   GO:0047499   GO:0005634   GO:0005764   GO:0005737   GO:0004623   GO:0102567   GO:0000302   GO:0016042   GO:0102568   GO:0005615   GO:0016209   GO:0016491   GO:0030126   GO:0005488   GO:0003677   GO:0003707   GO:0007169   GO:0016021   GO:0055114  

Subcellular location

Cytoplasm   Also found in lung secretory organelles (lamellar bodies).   With evidence from 8 publications.
Lysosome   Also found in lung secretory organelles (lamellar bodies).   With evidence from 8 publications.

Length:

223

Number of predicted TMHs:

0

Exp number of AAs in TMHs:

0.00782

Exp number, first 60 AAs:

0.00782

Total prob of N-in:

0.00955

outside

1  -  223

 

 

Pi

13.93521

Theta

16.214054

Tajima's D

-0.942041

CLR

0.304731

CSRT

0.145342732863357

Interpretation

Uncertain