ahpC:Gene Product(s) - EcoliWiki
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ahpC:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

AhpC

Synonyms

alkyl hydroperoxide reductase, C22 subunit[1], B0605[2][1], AhpC[2][1], Ssi8[2][1]

Product description

AhpC component[2][3];

Component of ; alkylhydroperoxide reductase[3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0004601

peroxidase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0575

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016209

antioxidant activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000866
SP_KW:KW-0049

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016491

oxidoreductase activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000866
SP_KW:KW-0560

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0051920

peroxiredoxin activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.11.1.15

F

Seeded from EcoCyc 12.5 [4]

complete

Under review

GO:0005624

membrane fraction

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required field missing

GO:0006805

xenobiotic metabolic process

PMID:7644465[6]

IMP: Inferred from Mutant Phenotype

P

tetralin, cyclohexane and proplybenze catabolism.

complete

GO:0004601

peroxidase activity

PMID:11717276[7]

IGI: Inferred from Genetic Interaction

EcoliWiki:katG

F

complete

GO:0051920

peroxiredoxin activity

PMID:7644465[6]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005737

cytoplasm

PMID:7499381[8]

IDA: Inferred from Direct Assay

C

complete

GO:0016209

antioxidant activity

PMID:7644465[6]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0016684

oxidoreductase activity, acting on peroxide as acceptor

PMID:7644465[6]

IMP: Inferred from Mutant Phenotype

F

complete

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Interactions

Partner TypePartnerNotesReferences

Protein

Subunits of alkylhydroperoxide reductase

could be indirect


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Notes

Localization

CompartmentDescriptionEvidenceNotes

cytoplasm


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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS
LDLVGKI
Mol. Wt

20.76 kDa (calc) [2]

pI
Extinction coefficient

23950 - 24200 (calc based on 5 Y, 3 W, and 2 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes

Domain

2 - 157

Thioredoxin

UniProt:P0AE08

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Structure

Structures
  • Representative homolog:
    2C0D|A (Plasmodium falciparum)
    24-208 of 187 residues (E-value: 1.2e-22) (Percent Identity: 28.88)
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Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:EG11384-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:P0AE08

UniProt (EcoliWiki Page)

UniProt:P0AE08

PFAM (EcoliWiki Page)

PFAM:PF00578

RefSeq (EcoliWiki Page)

RefSeq:NP_415138

ModBase (EcoliWiki Page)

ModBase:P0AE08

PDB (EcoliWiki Page)

PDB:1KYG


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Notes

Links

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NameURLComments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. 4.0 4.1 4.2 4.3 4.4 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed EcoliWiki page
  6. 6.0 6.1 6.2 6.3 Ferrante AA et al. (1995) Cloning of an organic solvent-resistance gene in Escherichia coli: the unexpected role of alkylhydroperoxide reductase. Proc Natl Acad Sci U S A 92: 7617-21 PubMed EcoliWiki page
  7. Seaver LC & Imlay JA (2001) Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J Bacteriol 183: 7173-81 PubMed EcoliWiki page
  8. Cha MK et al. (1995) Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli. J Biol Chem 270: 28635-41 PubMed EcoliWiki page


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