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:RIDA

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ridA (synonyms: yjgF)
Protein Name(s) 2-iminobutanoate/2-iminopropanoate deaminase

Enamine/imine deaminase

External Links
UniProt P0AF93
EMBL U14003
U00096
AP009048
RefSeq NP_418664.2
YP_492383.1
PDB 1QU9
PDBsum 1QU9
ProteinModelPortal P0AF93
SMR P0AF93
DIP DIP-36232N
STRING 511145.b4243
SWISS-2DPAGE P0AF93
PaxDb P0AF93
PRIDE P0AF93
EnsemblBacteria AAC77200
BAE78242
GeneID 12933726
948771
KEGG ecj:Y75_p4128
eco:b4243
PATRIC 32124063
EchoBASE EB2415
EcoGene EG12524
eggNOG COG0251
HOGENOM HOG000267215
InParanoid P0AF93
KO K09022
OMA FFDEHNV
OrthoDB EOG6QVRPF
PhylomeDB P0AF93
BioCyc EcoCyc:G7877-MONOMER
ECOL316407:JW5755-MONOMER
EvolutionaryTrace P0AF93
PRO PR:P0AF93
Proteomes UP000000318
UP000000625
Genevestigator P0AF93
GO GO:0005737
GO:0016020
GO:0019239
GO:0016787
GO:0009097
GO:0009636
Gene3D 3.30.1330.40
InterPro IPR013813
IPR006056
IPR019897
IPR006175
PANTHER PTHR11803
Pfam PF01042
SUPFAM SSF55298
TIGRFAMs TIGR00004
PROSITE PS01094

Annotations

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

enables

GO:0019239

deaminase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q7CP78

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1901565

organonitrogen compound catabolic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000211014
UniProtKB:P52758

P

Seeded From UniProt

complete

enables

GO:0019239

deaminase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12524
PANTHER:PTN000211014
TAIR:locus:2092374
UniProtKB:P37552
UniProtKB:P52758
UniProtKB:Q7CP78

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG12524
PANTHER:PTN000211014
RGD:70940
SGD:S000000859

C

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:25517874[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:10595546[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019239

deaminase activity

PMID:23696645[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019239

deaminase activity

PMID:22094463[6]

ECO:0000266

sequence orthology evidence used in manual assertion

UniProtKB:Q7CP78

F

Seeded From UniProt

complete

involved_in

GO:0009636

response to toxic substance

PMID:25517874[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0009636

response to toxic substance

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0216

P

Seeded From UniProt

complete

involved_in

GO:0009082

branched-chain amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0100

P

Seeded From UniProt

complete

involved_in

GO:0009097

isoleucine biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0412

P

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

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

Notes

References

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

  1. 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
  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. 3.0 3.1 Müller, A et al. (2014) Activation of RidA chaperone function by N-chlorination. Nat Commun 5 5804 PubMed GONUTS page
  4. Volz, K (1999) A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli. Protein Sci. 8 2428-37 PubMed GONUTS page
  5. Lindemann, C et al. (2013) Redox proteomics uncovers peroxynitrite-sensitive proteins that help Escherichia coli to overcome nitrosative stress. J. Biol. Chem. 288 19698-714 PubMed GONUTS page
  6. Lambrecht, JA et al. (2012) Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5'-phosphate (PLP)-dependent enzyme reactions. J. Biol. Chem. 287 3454-61 PubMed GONUTS page
  7. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  8. 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