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ECOLI:BGLR

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) uidA (synonyms: gurA, gusA)
Protein Name(s) Beta-glucuronidase

GUS Beta-D-glucuronoside glucuronosohydrolase

External Links
UniProt P05804
EMBL M14641
S69414
U00096
AP009048
PIR C64918
RefSeq NP_416134.1
YP_489880.1
PDB 3K46
3K4A
3K4D
3LPF
3LPG
4JHZ
PDBsum 3K46
3K4A
3K4D
3LPF
3LPG
4JHZ
ProteinModelPortal P05804
SMR P05804
DIP DIP-11086N
IntAct P05804
STRING 511145.b1617
CAZy GH2
PRIDE P05804
EnsemblBacteria AAC74689
BAA15368
GeneID 12934489
946149
KEGG ecj:Y75_p1593
eco:b1617
PATRIC 32118536
EchoBASE EB1048
EcoGene EG11055
eggNOG COG3250
HOGENOM HOG000120896
InParanoid P05804
KO K01195
OMA NRQPKQV
OrthoDB EOG6DRPFW
PhylomeDB P05804
BioCyc EcoCyc:BETA-GLUCURONID-MONOMER
ECOL316407:JW1609-MONOMER
MetaCyc:BETA-GLUCURONID-MONOMER
SABIO-RK P05804
EvolutionaryTrace P05804
PRO PR:P05804
Proteomes UP000000318
UP000000625
Genevestigator P05804
GO GO:0004566
GO:0019391
Gene3D 2.60.120.260
2.60.40.320
3.20.20.80
InterPro IPR008979
IPR006101
IPR013812
IPR023232
IPR023230
IPR006102
IPR006104
IPR006103
IPR013781
IPR017853
Pfam PF00703
PF02836
PF02837
PRINTS PR00132
SUPFAM SSF49303
SSF49785
SSF51445
PROSITE PS00719
PS00608

Annotations

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

enables

GO:0030246

carbohydrate binding

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000007255
RGD:2772

F

Seeded From UniProt

complete

involved_in

GO:0019391

glucuronoside catabolic process

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11055
PANTHER:PTN000007255

P

Seeded From UniProt

complete

enables

GO:0004566

beta-glucuronidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11055
FB:FBgn0270927
MGI:MGI:95872
PANTHER:PTN000007255
RGD:2772

F

Seeded From UniProt

complete

involved_in

GO:0051289

protein homotetramerization

PMID:21051639[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21051639[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019391

glucuronoside catabolic process

PMID:4568840[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17309111[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004566

beta-glucuronidase activity

PMID:3105604[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004553

hydrolase activity, hydrolyzing O-glycosyl compounds

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006101
InterPro:IPR006102
InterPro:IPR006103
InterPro:IPR006104

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006101
InterPro:IPR006102
InterPro:IPR006103
InterPro:IPR006104

P

Seeded From UniProt

complete

enables

GO:0004566

beta-glucuronidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.2.1.31

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

P

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

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

Notes

References

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

  1. 1.0 1.1 1.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. 2.0 2.1 Wallace, BD et al. (2010) Alleviating cancer drug toxicity by inhibiting a bacterial enzyme. Science 330 831-5 PubMed GONUTS page
  3. Novel, G & Novel, M (1973) [Mutants of E. coli K 12 unable to grow on methyl-beta-D-glucuronide: map l ocation of uid A. locus of the structural gene of beta-D-glucuronidase]. Mol. Gen. Genet. 120 319-35 PubMed GONUTS page
  4. Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  5. Blanco, C & Nemoz, G (1987) One step purification of Escherichia coli beta-glucuronidase. Biochimie 69 157-61 PubMed GONUTS page