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ECOLI:PAAG

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) paaG (synonyms: ydbT)
Protein Name(s) 1,2-epoxyphenylacetyl-CoA isomerase
External Links
UniProt P77467
EMBL X97452
U00096
AP009048
PIR E64890
RefSeq NP_415912.1
YP_489663.1
PDB 4FZW
PDBsum 4FZW
ProteinModelPortal P77467
SMR P77467
IntAct P77467
STRING 511145.b1394
PRIDE P77467
EnsemblBacteria AAC74476
BAA15000
GeneID 12931975
946263
KEGG ecj:Y75_p1371
eco:b1394
PATRIC 32118074
EchoBASE EB3504
EcoGene EG13741
eggNOG COG1024
HOGENOM HOG000027949
InParanoid P77467
KO K15866
OMA AIKRAMH
OrthoDB EOG6M9F0M
PhylomeDB P77467
BioCyc EcoCyc:G6715-MONOMER
ECOL316407:JW1389-MONOMER
MetaCyc:G6715-MONOMER
UniPathway UPA00930
PRO PR:P77467
Proteomes UP000000318
UP000000625
Genevestigator P77467
GO GO:0042802
GO:0016853
GO:0016829
GO:0010124
Gene3D 1.10.12.10
3.90.226.10
InterPro IPR029045
IPR014748
IPR001753
IPR011968
Pfam PF00378
SUPFAM SSF52096
TIGRFAMs TIGR02280

Annotations

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

enables

GO:0016853

isomerase activity

PMID:20660314[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG13741
PANTHER:PTN001733184

F

Seeded From UniProt

complete

involved_in

GO:0006635

fatty acid beta-oxidation

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:94871
PANTHER:PTN000941828
RGD:69330
UniProtKB:P30084

P

Seeded From UniProt

complete

enables

GO:0004300

enoyl-CoA hydratase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG13740
MGI:MGI:1338011
PANTHER:PTN000941828
RGD:69330
UniProtKB:P30084
UniProtKB:Q13825

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22961985[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010124

phenylacetate catabolic process

PMID:12846838[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001753

F

Seeded From UniProt

complete

involved_in

GO:0010124

phenylacetate catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011968

P

Seeded From UniProt

complete

enables

GO:0016853

isomerase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0413

F

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0010124

phenylacetate catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00930

P

Seeded From UniProt

complete

Notes

References

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

  1. Teufel, R et al. (2010) Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc. Natl. Acad. Sci. U.S.A. 107 14390-5 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Grishin, AM et al. (2012) Protein-protein interactions in the β-oxidation part of the phenylacetate utilization pathway: crystal structure of the PaaF-PaaG hydratase-isomerase complex. J. Biol. Chem. 287 37986-96 PubMed GONUTS page
  4. Ismail, W et al. (2003) Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Eur. J. Biochem. 270 3047-54 PubMed GONUTS page