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ECOLI:YIGB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) yigB
Protein Name(s) Flavin mononucleotide phosphatase YigB

FMN phosphatase

External Links
UniProt P0ADP0
EMBL M38257
M87049
U00096
AP009048
X00738
PIR D37841
RefSeq NP_418257.1
YP_491629.1
ProteinModelPortal P0ADP0
SMR P0ADP0
DIP DIP-48086N
STRING 511145.b3812
PaxDb P0ADP0
EnsemblBacteria AAC76815
BAE77488
GeneID 12934289
948357
KEGG ecj:Y75_p3365
eco:b3812
PATRIC 32123125
EchoBASE EB1187
EcoGene EG11202
eggNOG COG1011
HOGENOM HOG000248345
InParanoid P0ADP0
KO K07025
OMA YHPALRD
OrthoDB EOG6W19QD
PhylomeDB P0ADP0
BioCyc EcoCyc:EG11202-MONOMER
ECOL316407:JW3785-MONOMER
MetaCyc:EG11202-MONOMER
PRO PR:P0ADP0
Proteomes UP000000318
UP000000625
Genevestigator P0ADP0
GO GO:0043726
GO:0000287
GO:0016791
GO:0016311
GO:0022611
GO:0009231
Gene3D 3.40.50.1000
InterPro IPR023214
IPR006439
Pfam PF00702
SUPFAM SSF56784
TIGRFAMs TIGR01549

Annotations

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

enables

GO:0000287

magnesium ion binding

PMID:16990279[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0043726

5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity

PMID:24123841[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0022611

dormancy process

PMID:18519731[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0016791

phosphatase activity

PMID:16990279[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009231

riboflavin biosynthetic process

PMID:24123841[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016311

dephosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0016791

P

Seeded From UniProt

complete

involved_in

GO:0016311

dephosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0043726

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006439

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

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0009231

riboflavin biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00275

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Kuznetsova, E et al. (2006) Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J. Biol. Chem. 281 36149-61 PubMed GONUTS page
  2. 2.0 2.1 Haase, I et al. (2013) Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis. Chembiochem 14 2272-5 PubMed GONUTS page
  3. Hansen, S et al. (2008) Role of global regulators and nucleotide metabolism in antibiotic tolerance in Escherichia coli. Antimicrob. Agents Chemother. 52 2718-26 PubMed GONUTS page