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ECOLI:PTA

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Contents

Species (Taxon ID) Escherichia coli (strain K12). ([1])
Gene Name(s) pta
Protein Name(s) Phosphate acetyltransferase

Phosphotransacetylase

External Links
EMBL D17576
D21123
U00096
AP009048
PIR G65001
JX0357
S50130
RefSeq AP_002897.1
NP_416800.1
ProteinModelPortal P0A9M8
SMR P0A9M8
DIP DIP-35815N
IntAct P0A9M8
MINT MINT-1263208
PhosSite P0A9M8
SWISS-2DPAGE P0A9M8
PRIDE P0A9M8
EnsemblBacteria EBESCT00000004864
EBESCT00000018341
GeneID 946778
GenomeReviews AP009048_GR
U00096_GR
KEGG ecj:JW2294
eco:b2297
EchoBASE EB4147
EcoGene EG20173
eggNOG COG0857
GeneTree EBGT00050000008963
HOGENOM HBG576804
OMA KPIAQPH
ProtClustDB PRK05632
BioCyc EcoCyc:PHOSACETYLTRANS-MON
MetaCyc:PHOSACETYLTRANS-MON
Genevestigator P0A9M8
GO GO:0005737
GO:0008959
GO:0005515
GO:0008270
GO:0019413
GO:0045733
GO:0019427
GO:0070689
InterPro IPR010766
IPR016475
IPR004614
IPR002505
Pfam PF07085
PF01515
PIRSF PIRSF006107
TIGRFAMs TIGR00651

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005515

protein binding

PMID:15690043[1]

IPI: Inferred from Physical Interaction

UniProtKB:P0A9I5

F

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded From UniProt

GO:0005737

cytoplasm

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0086

C

Seeded From UniProt

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002505

P

Seeded From UniProt

GO:0008270

zinc ion binding

PMID:11985624[2]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

GO:0008959

phosphate acetyltransferase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016475

F

Seeded From UniProt

GO:0008959

phosphate acetyltransferase activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.3.1.8

F

Seeded From UniProt

GO:0008959

phosphate acetyltransferase activity

PMID:13535743[3]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

GO:0008959

phosphate acetyltransferase activity

PMID:20236319[4]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

GO:0016407

acetyltransferase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004614

F

Seeded From UniProt

GO:0016740

transferase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0808

F

Seeded From UniProt

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0012

F

Seeded From UniProt

GO:0019413

acetate biosynthetic process

PMID:21941[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0019427

acetyl-CoA biosynthetic process from acetate

PMID:21941[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0045733

acetate catabolic process

PMID:21941[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0070689

L-threonine catabolic process to propionate

PMID:9484901[6]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0006083

acetate metabolic process

PMID:21941[5]

IMP: Inferred from Mutant Phenotype

P

Fig 1: Showed decreased acetate production in mutant phenotype.

complete

GO:0042710

biofilm formation

PMID:12753190[7]

IMP: Inferred from Mutant Phenotype

P

Fig 6: Shows the ackA biofilm is much thinner than both the WT and the ackA-pta mutant.

complete

Notes

References

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

  1. Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed GONUTS page
  2. Katayama A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur J Biochem 269: 2403-13 PubMed GONUTS page
  3. GOLDMAN DS (1958) Purification of phosphotransacetylase from Escherichia coli, K-12. Biochim Biophys Acta 28: 436-7 PubMed GONUTS page
  4. Campos-Bermudez VA et al. (2010) Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation. FEBS J 277: 1957-66 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 Brown TD et al. (1977) The enzymic interconversion of acetate and acetyl-coenzyme A in Escherichia coli. J Gen Microbiol 102: 327-36 PubMed GONUTS page
  6. Hesslinger C et al. (1998) Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol Microbiol 27: 477-92 PubMed GONUTS page
  7. Wolfe AJ et al. (2003) Evidence that acetyl phosphate functions as a global signal during biofilm development. Mol Microbiol 48: 977-88 PubMed GONUTS page
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