SGID Silkworm Genome Informatics Database
Gene
KWMTBOMO15852  Validated by peptides from experiments
Pre Gene Modal
BGIBMGA000064
Annotation
thioredoxin_peroxidase_[Bombyx_mori]
Full name
Thioredoxin-dependent peroxide reductase, mitochondrial      
Alternative Name
Peroxiredoxin-3
Location in the cell
Cytoplasmic   Reliability : 1.294 Mitochondrial   Reliability : 1.457
 

Sequence

CDS
ATGTCGTTCATTGTGAAGCAACTAAGTCGAAGTGTACTGTCGCCGGCTTTCAAAGTAGCAAAAAGGATTAATTTTTCTACGACCAGCACTACAAGAGCTCCTAAAGTTCAGAAGCCTGCTCCAGACTTCAGTGCGACAGCAGTTGTCAATGGAGAGTTCAATCAACTTAAACTTTCAGATTTCACGGGAAAATACGTAGTTCTGTTCTTCTATCCATTGGATTTCACATTTGTATGTCCGACAGAGCTCATAGCGTTCAGTGATAAAGCTAAAGACTTTGCTGGAATCGATTGTCAGGTGATTGGAGTGTCCACAGACTCTGAGTTCAGTCATCTCGCATGGATCAACACTCCTAGGAAGGACGGTGGATTGGGAAAAATGGAAATTCCTCTGCTTGCTGATTACAAAAAACAGATTTCAAAAGATTATGATGTATTACTTGATGATGGGTTTGCATTAAGAGGTTTGTTCATAATCGACCGTAATGGCACCCTGCGTCACATGTCGGTGAACGATCTGCCCGTGGGCCGCTCCGTGGACGAGACGCTCCGCCTGGTCAAGGCCTTCCAGTTCGCCGACAAGCACGGAGAGGTGTGCCCGGCCGGCTGGAACCCGGACACCAACGCCGACACCATCAAGCCGAACCCCAAGGACAGTAAAGAATACTTTCAAAAAGCTAATTAA
Protein
MSFIVKQLSRSVLSPAFKVAKRINFSTTSTTRAPKVQKPAPDFSATAVVNGEFNQLKLSDFTGKYVVLFFYPLDFTFVCPTELIAFSDKAKDFAGIDCQVIGVSTDSEFSHLAWINTPRKDGGLGKMEIPLLADYKKQISKDYDVLLDDGFALRGLFIIDRNGTLRHMSVNDLPVGRSVDETLRLVKAFQFADKHGEVCPAGWNPDTNADTIKPNPKDSKEYFQKAN

Summary

Description
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
Catalytic Activity
[protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O
Subunit
Homodimer; disulfide-linked, upon oxidation. 6 homodimers assemble to form a ring-like dodecamer. Interacts with NEK6. Interacts with LRRK2. Interacts with RPS6KC1 (via PX domain).
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 typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.
Similarity
Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
Keywords
Acetylation   Antioxidant   Complete proteome   Cytoplasm   Disulfide bond   Endosome   Mitochondrion   Oxidoreductase   Peroxidase   Phosphoprotein   Redox-active center   Reference proteome   Transit peptide  
Feature
chain  Thioredoxin-dependent peroxide reductase, mitochondrial
EC Number
1.11.1.15
EMBL
DQ443351    ABF51440.1    BABH01035692    NWSH01000019    PCG80726.1    MF805701    + More
AWA45766.1    JQ285933    AFO67940.1    ODYU01000131    SOQ34389.1    AGBW02009638    OWR50269.1    MF979107    AWA45970.1    KQ461111    KPJ08942.1    AK401507    KQ459144    BAM18129.1    KPJ03608.1    GAIX01003570    JAA88990.1    AXCM01002712    UFQT01000555    SSX25257.1    GQ252681    ADI78066.1    AAAB01008846    EAA06406.3    AAPE02042232    APCN01001346    UFQS01004076    UFQT01004076    SSX16159.1    SSX35485.1    DS232072    EDS33918.1    GFDL01008412    JAV26633.1    ATLV01012458    KE524793    KFB36809.1    CP026257    AWP14350.1    GCES01034363    JAR51960.1    KU207097    APG79659.1    KC990696    KF270681    AGT56738.1    AGW80514.1    KQ042804    KKF10455.1    GCES01141934    JAQ44388.1    KM370333    AJC98155.1    BT083182    ACQ58889.1    HAEB01015527    HAEC01001294    SBQ62054.1    AERX01006552    AERX01006553    BT075596    ACO10020.1    HADW01006134    HADX01009574    SBP07534.1    KR905163    AKZ42351.1    HAEE01013405    SBR33455.1    HAEH01015333    SBS02477.1    AJVK01000890    HAEF01012036    HAEG01011003    SBR53195.1    HAEI01013736    SBS16205.1    GFFV01003995    JAV35950.1    HADY01019343    HAEJ01003748    SBP57828.1    HADZ01020705    HAEA01001370    SBQ29850.1    NDHI03003398    PNJ65458.1    CR857380    ADFV01164449    ADFV01164450    ADFV01164451    KB031059    ELK04914.1    RJVU01057857    ROK15673.1    AYCK01011665    AEFK01004544    CH478048    EAT34216.1    GBYX01237987    JAO65174.1    AAKN02003057    KR086406    ALG02339.1    BT046676    ACI66477.1    JSUE03044428   
Pfam
PF10417   1-cysPrx_C        + More
PF00578   AhpC-TSA
Interpro
IPR036249   Thioredoxin-like_sf        + More
IPR024706   Peroxiredoxin_AhpC-typ       
IPR000866   AhpC/TSA       
IPR013766   Thioredoxin_domain       
IPR019479   Peroxiredoxin_C       
SUPFAM
SSF52833   SSF52833       
PDB
5JCG     E-value=1.51793e-77,     Score=734

Ontologies

Topology

Subcellular location
Mitochondrion   Localizes to early endosomes in a RPS6KC1-dependent manner.   With evidence from 2 publications.
Cytoplasm   Localizes to early endosomes in a RPS6KC1-dependent manner.   With evidence from 2 publications.
Early endosome   Localizes to early endosomes in a RPS6KC1-dependent manner.   With evidence from 2 publications.
Length:
227
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
2.73881
Exp number, first 60 AAs:
0.00064
Total prob of N-in:
0.15869
outside
1  -  227
 
 

Population Genetic Test Statistics

Pi
61.996218
Theta
136.911751
Tajima's D
-0.575414
CLR
50.226635
CSRT
0.222288885555722
Interpretation
Uncertain

Multiple alignment of Orthologues

 
 

Gene Tree

 
 
Peptides ×
Source Sequence Identity Evalue
26280517 AIYKDPFRR 96.67 4e-16
25044914 AKDEFPGFIDDIVK 96.67 4e-16
28467696 AKDEFPGFIDDIVK 96.67 4e-16
25044914 DFAETQVIVK 96.43 5e-15
28467696 DFAEIKR 96.43 5e-15
26822097 HMSVNDIPVGR 100.00 2e-12
26280517 HGAFCIETQNYPDAVHHTNFPR 100.00 2e-12
28467696 HGESQPIVGHEPITAK 100.00 2e-12
28556443 AFQFADK 100.00 2e-12
28556443 VQKPAPDFSATAVVNGEFNQLK 100.00 7e-09
28556443 MEIPLLADYK 100.00 7e-09
28556443 MEIPLLADYKK 100.00 7e-09
26822097 MEIPIIADYK 95.45 1e-08
26280517 VQEPIAAN 95.45 1e-08
28556443 SLIQAICEHALFGPER 100.00 0.014
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