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ECOLI:PTA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pta
Protein Name(s) Phosphate acetyltransferase

Phosphotransacetylase

External Links
UniProt P0A9M8
EMBL D17576
D21123
U00096
AP009048
PIR G65001
JX0357
S50130
RefSeq NP_416800.1
YP_490539.1
ProteinModelPortal P0A9M8
SMR P0A9M8
DIP DIP-35815N
IntAct P0A9M8
MINT MINT-1263208
STRING 511145.b2297
PhosSite P0810425
SWISS-2DPAGE P0A9M8
PaxDb P0A9M8
PRIDE P0A9M8
EnsemblBacteria AAC75357
BAA16136
GeneID 12932506
946778
KEGG ecj:Y75_p2263
eco:b2297
PATRIC 32119965
EchoBASE EB4147
EcoGene EG20173
eggNOG COG0280
HOGENOM HOG000053797
InParanoid P0A9M8
KO K13788
OMA KPIAQPH
OrthoDB EOG6BKJ5W
PhylomeDB P0A9M8
BioCyc EcoCyc:PHOSACETYLTRANS-MONOMER
ECOL316407:JW2294-MONOMER
MetaCyc:PHOSACETYLTRANS-MONOMER
UniPathway UPA00340
PRO PR:P0A9M8
Proteomes UP000000318
UP000000625
Genevestigator P0A9M8
GO GO:0005737
GO:0008959
GO:0008270
GO:0019413
GO:0045733
GO:0006083
GO:0019427
GO:0070689
Gene3D 3.40.1390.20
3.40.50.300
InterPro IPR010766
IPR016475
IPR027417
IPR004614
IPR002505
IPR028979
Pfam PF07085
PF01515
PIRSF PIRSF006107
SUPFAM SSF52540
SSF75138
TIGRFAMs TIGR00651

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006083

acetate metabolic process

PMID:21941[1]

ECO:0000315

P

Fig 1: Showed decreased acetate production in mutant phenotype.

complete
CACAO 1991

involved_in

GO:0006083

acetate metabolic process

PMID:21941[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:11985624[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0070689

L-threonine catabolic process to propionate

PMID:9484901[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045733

acetate catabolic process

PMID:21941[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019427

acetyl-CoA biosynthetic process from acetate

PMID:21941[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019413

acetate biosynthetic process

PMID:21941[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008959

phosphate acetyltransferase activity

PMID:20236319[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008959

phosphate acetyltransferase activity

PMID:13535743[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008959

phosphate acetyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016475

F

Seeded From UniProt

complete

enables

GO:0016407

acetyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004614

F

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002505

F

Seeded From UniProt

complete

enables

GO:0008959

phosphate acetyltransferase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:2.3.1.8

F

Seeded From UniProt

complete

enables

GO:0016746

transferase activity, transferring acyl groups

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0012

F

Seeded From UniProt

complete

enables

GO:0016740

transferase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0808

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

involved_in

GO:0006085

acetyl-CoA biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00340

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 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
  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. 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
  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. GOLDMAN, DS (1958) Purification of phosphotransacetylase from Escherichia coli, K-12. Biochim. Biophys. Acta 28 436-7 PubMed GONUTS page
  6. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  7. 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