yigB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

YigB

Synonyms

predicted hydrolase[1], B3812[2][1], YigB[2][1] , ECK3807, JW3785, b3812

Product description

FMN phosphatase[2][3]

FMN phosphatase; physiological role unknown; HAD7[4]

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0043726

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

PMID:24123841[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc

complete

GO:0005829

cytosol

PMID:19054114[6]

IEA: Inferred from Electronic Annotation

C

Seeded from EcoCyc

Missing: with/from

GO:0009231

riboflavin biosynthetic process

PMID:24123841[5]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence
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Notes

Localization

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Compartment Description Evidence Reference/Source Notes
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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc 

MRFYRPLGRI SALTFDLDDT LYDNRPVILR TEREALTFVQ NYHPALRSFQ NEDLQRLRQA
VREAEPEIYH DVTRWRFRSI EQAMLDAGLS AEEASAGAHA AMINFAKWRS RIDVPQQTHD
TLKQLAKKWP LVAITNGNAQ PELFGLGDYF EFVLRAGPHG RSKPFSDMYF LAAEKLNVPI
GEILHVGDDL TTDVGGAIRS GMQACWIRPE NGDLMQTWDS RLLPHLEISR LASLTSLI
Length

238

Mol. Wt

27.122 kDa

pI

6.4 (calculated)

Extinction coefficient

36,440 - 36,565 (calc based on 6 Y, 5 W, and 1 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

10..201

PF00702 haloacid dehalogenase-like hydrolase

PMID:19920124[7]

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Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=yigB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16131664

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:948357

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0012450

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0ADP0

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11202

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11202

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:948357

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001182

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1187

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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

  1. ↑ 1.0 1.1 1.2 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ 5.0 5.1 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
  6. ↑ Díaz-Mejía, JJ et al. (2009) Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome. FEMS Microbiol. Rev. 33 66-97 PubMed
  7. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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