GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

ECOLI:AHPC

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ahpC
Protein Name(s) Alkyl hydroperoxide reductase subunit C

Alkyl hydroperoxide reductase protein C22 Peroxiredoxin SCRP-23 Sulfate starvation-induced protein 8 SSI8 Thioredoxin peroxidase

External Links
UniProt P0AE08
EMBL D13187
U82598
U00096
AP009048
PIR C64794
RefSeq NP_415138.1
YP_488895.1
ProteinModelPortal P0AE08
SMR P0AE08
BioGrid 849610
DIP DIP-36164N
IntAct P0AE08
MINT MINT-1241588
STRING 511145.b0605
PeroxiBase 4830
PhosSite P0809369
SWISS-2DPAGE P0AE08
PaxDb P0AE08
PRIDE P0AE08
EnsemblBacteria AAC73706
BAA35235
GeneID 12930899
945225
KEGG ecj:Y75_p0595
eco:b0605
PATRIC 32116388
EchoBASE EB1357
EcoGene EG11384
eggNOG COG0450
HOGENOM HOG000022343
InParanoid P0AE08
KO K03386
OMA FHKGEFV
OrthoDB EOG67X1XH
PhylomeDB P0AE08
BioCyc EcoCyc:EG11384-MONOMER
ECOL316407:JW0598-MONOMER
MetaCyc:EG11384-MONOMER
PRO PR:P0AE08
Proteomes UP000000318
UP000000625
Genevestigator P0AE08
GO GO:0005737
GO:0005829
GO:0016020
GO:0032843
GO:0042802
GO:0016684
GO:0004601
GO:0051920
GO:0009970
GO:0033214
GO:0033195
GO:0033194
Gene3D 3.40.30.10
InterPro IPR017559
IPR000866
IPR024706
IPR019479
IPR012336
Pfam PF10417
PF00578
PIRSF PIRSF000239
SUPFAM SSF52833
TIGRFAMs TIGR03137
PROSITE PS51352

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0019290

siderophore biosynthetic process

PMID:23042987[1]

ECO:0000315

P

Fig 2B,C&D, Fig 4, Fig 5, Fig 6, Table 3

complete
CACAO 5652

involved_in

GO:0019290

siderophore biosynthetic process

PMID:23042987[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0040309
MGI:MGI:1859815
PANTHER:PTN000073874
PomBase:SPCC576.03c
SGD:S000002861
SGD:S000004490
UniProtKB:P9WQB7

P

Seeded From UniProt

complete

involved_in

GO:0042744

hydrogen peroxide catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000189947
FB:FBgn0040308
FB:FBgn0040309
MGI:MGI:109486
PANTHER:PTN000073874
PomBase:SPCC576.03c
UniProtKB:Q06830
UniProtKB:Q6ER94

P

Seeded From UniProt

complete

involved_in

GO:0033214

siderophore-dependent iron import into cell

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11384
PANTHER:PTN000074131

P

Seeded From UniProt

complete

enables

GO:0008379

thioredoxin peroxidase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000189947
FB:FBgn0040308
FB:FBgn0040309
PANTHER:PTN000073874
PomBase:SPCC576.03c
SGD:S000002861
SGD:S000004490
UniProtKB:P32119
UniProtKB:Q06830
UniProtKB:Q8I5Q6
UniProtKB:Q8IL80

F

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0040308
FB:FBgn0040309
MGI:MGI:99523
PANTHER:PTN000073874
RGD:3838
RGD:620039
UniProtKB:P32119
UniProtKB:Q8I5Q6
UniProtKB:Q8IL80

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11384
FB:FBgn0040308
FB:FBgn0040309
MGI:MGI:1859815
PANTHER:PTN000073874
RGD:3838
RGD:620039
SGD:S000004490
UniProtKB:Q8IL80

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:24561554[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AE08

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0AE08

F

Seeded From UniProt

complete

enables

GO:0032843

hydroperoxide reductase activity

PMID:7644465[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016684

oxidoreductase activity, acting on peroxide as acceptor

PMID:7644465[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009970

cellular response to sulfate starvation

PMID:8774726[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:7499381[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004601

peroxidase activity

PMID:11717276[8]

ECO:0000316

genetic interaction evidence used in manual assertion

EcoliWiki:katG

F

Seeded From UniProt

complete

involved_in

GO:0033195

response to alkyl hydroperoxide

PMID:2649484[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0033194

response to hydroperoxide

PMID:7733872[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009321

alkyl hydroperoxide reductase complex

PMID:25372677[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0016209

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0051920

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004601

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0008379

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0016209

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004601

P

Seeded From UniProt

complete

involved_in

GO:0098869

cellular oxidant detoxification

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0051920

P

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017559

P

Seeded From UniProt

complete

enables

GO:0016209

antioxidant activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000866

F

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000866

F

Seeded From UniProt

complete

involved_in

GO:0045454

cell redox homeostasis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013766

P

Seeded From UniProt

complete

enables

GO:0051920

peroxiredoxin activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR017559
InterPro:IPR019479

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000866
InterPro:IPR017559
InterPro:IPR019479

P

Seeded From UniProt

complete

enables

GO:0051920

peroxiredoxin activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.11.1.15

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016209

antioxidant activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0049

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

enables

GO:0004601

peroxidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0575

F

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Ma, L & Payne, SM (2012) AhpC is required for optimal production of enterobactin by Escherichia coli. J. Bacteriol. 194 6748-57 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 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 GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 3.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
  5. ↑ 5.0 5.1 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 GONUTS page
  6. ↑ Quadroni, M et al. (1996) Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli. Eur. J. Biochem. 239 773-81 PubMed GONUTS page
  7. ↑ Cha, MK et al. (1995) Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli. J. Biol. Chem. 270 28635-41 PubMed GONUTS page
  8. ↑ 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 GONUTS page
  9. ↑ Storz, G et al. (1989) An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J. Bacteriol. 171 2049-55 PubMed GONUTS page
  10. ↑ Tsuji, K et al. (1995) Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli. Biochem. J. 307 ( Pt 2) 377-81 PubMed GONUTS page
  11. ↑ Dip, PV et al. (2014) Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 70 2848-62 PubMed GONUTS page
  12. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  13. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=ECOLI:AHPC&oldid=5953126"