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ybhA: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

YbhA

Synonyms

predicted hydrolase[1], YbhA[2][1], B0766[2][1], fructose 1,6-bisphosphatase III[2][1]

Product description

EG11239[2][3]

Pyridoxal phosphate (PLP) phosphatase; phosphoramidase; physiological role unknown; HAD14[4]

EC number (for enzymes)


Notes

Function

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

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc [5]

complete

GO:0016787

hydrolase activity

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR000150
SP_KW:KW-0378

F

Seeded from EcoCyc [5]

complete

Deprecated

GO:0016020

membrane

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

C

No membrane spanning segments were predicted for YbhA using TMHMM 3.0. This electronic annotation probably made because YbhA shares sequence similarity with the catalytic domain of P-type ATPases.

complete

Deprecated

GO:0015662

ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

F

YbhA has sequence similarity to only the catalytic domain of P-type ATPases. No predicted membrane spanning regions were identified in YbhA using TMHMM 3.0.

complete

GO:0008152

metabolic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000150
InterPro:IPR005834
InterPro:IPR006379

P

Seeded from EcoCyc [5]

complete

GO:0006810

transport

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

F

Seeded from EcoCyc [5]

complete

GO:0003824

catalytic activity

GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005834
InterPro:IPR006379

F

Seeded from EcoCyc [5]

complete

GO:0000287

magnesium ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc [5]

complete

GO:0042822

pyridoxal phosphate metabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006754

ATP biosynthetic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

P

Seeded from EcoCyc [5]

complete

Under review

GO:0042132

fructose 1,6-bisphosphate 1-phosphatase activity

PMID:16990279[7]

F

YbhA releases phosphate from fructose-1,6-bis-phosphate, but which phosphate is released wasn't determined.

required field missing

GO:0050308

sugar-phosphatase activity

PMID:16990279[7]

IDA: Inferred from Direct Assay

F

complete

GO:0050308

sugar-phosphatase activity

PMID:16889420[8]

IDA: Inferred from Direct Assay

F

complete

GO:0016773

phosphotransferase activity, alcohol group as acceptor

PMID:16889420[8]

IDA: Inferred from Direct Assay

F

Purified YbhA will form glycerol phosphate from glycerol and inorganic phosphate (Table 4). The authors note that the phosphotransferase activity is lower than the phosphatase activity, and that other mono-phosphates can serve as the phosphate donor.

complete

GO:0033883

pyridoxal phosphatase activity

PMID:16990279[7]

IDA: Inferred from Direct Assay

F

Figure 1 and Table 2.

complete

GO:0016791

phosphatase activity

PMID:16990279[7]

IDA: Inferred from Direct Assay

F

YbhA had phosphatase activity on 8 of the 80 phosphorylated compounds tested. These were (in decreasing order of activity): pyridoxal-5-P, erythrose-4-P, Fructose-1,6-bis-P, flavin mononucleotide (FMN), thiamine pyrophosphate, phosphoribosyl pyrophosphate (PRPP), Glucose-1,6-di-P, and 6-phosphogluconate (Fig. 1).

complete

GO:0000287

magnesium ion binding

PMID:16990279[7]

IDA: Inferred from Direct Assay

F

Km is 0.14±0.02 mM with pyridoxal-5-phosphate as the substrate (Suppl. Table 2).

complete

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

Partner TypePartnerNotesReferencesEvidence

Protein

groL

PMID:16606699[9]

Experiment(s):EBI-1137896

Protein

moaA

PMID:16606699[9]

Experiment(s):EBI-1137896

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

CompartmentDescriptionEvidenceSourceNotes

Notes

Structure and Physical Properties

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

Sequence

at EcoCyc

MTTRVIALDL DGTLLTPKKT LLPSSIEALA RAREAGYQLI IVTGRHHVAI HPFYQALALD
TPAICCNGTY LYDYHAKTVL EADPMPVIKA LQLIEMLNEH HIHGLMYVDD AMVYEHPTGH
VIRTSNWAQT LPPEQRPTFT QVASLAETAQ QVNAVWKFAL THDDLPQLQH FGKHVEHELG
LECEWSWHDQ VDIARGGNSK GKRLTKWVEA QGWSMENVVA FGDNFNDISM LEAAGTGVAM
GNADDAVKAR ANIVIGDNTT DSIAQFIYSH LI
Length

272

Mol. Wt

30.2 kDa

pI

5.8 (calculated)

Extinction coefficient

44,920 - 45,295 (calc based on 8 Y, 6 W, and 3 C residues)


Domains/Motifs/Modification Sites

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

TypeResiduesDescriptionNotesReferences


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

Structures
Models

View models at:

Structure figures

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 typeSourceNotes/Reference

Notes

Accessions in Other Databases

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

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:EG11239-MONOMER

UniProt (EcoliWiki Page)

UniProt:P21829

PFAM (EcoliWiki Page)

PFAM:PF00702

RefSeq (EcoliWiki Page)

RefSeq:NP_415287


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 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 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 5.2 5.3 5.4 5.5 5.6 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. 7.0 7.1 7.2 7.3 7.4 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 EcoliWiki page
  8. 8.0 8.1 Saito N et al. (2006) Metabolomics approach for enzyme discovery. J Proteome Res 5: 1979-87 PubMed EcoliWiki page
  9. 9.0 9.1 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page

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