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] , ECK0755, JW0749, modD, b0766

Product description

EG11239[2][3]

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

Under review

GO:0042132

fructose 1,6-bisphosphate 1-phosphatase activity

PMID:16990279[5]

F

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

Missing: evidence

GO:0000287

magnesium ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

PMID:16990279[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005834

F

Seeded from EcoCyc (v14.0)

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006379

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

F

Seeded from EcoCyc (v14.0)

complete

GO:0006754

ATP biosynthetic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

P

Seeded from EcoCyc (v14.0)

complete

GO:0050308

sugar-phosphatase activity

PMID:16990279[5]

IDA: Inferred from Direct Assay

F

complete

GO:0008152

metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000150

P

Seeded from EcoCyc (v14.0)

complete

GO:0008152

metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005834

P

Seeded from EcoCyc (v14.0)

complete

GO:0008152

metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006379

P

Seeded from EcoCyc (v14.0)

complete

GO:0015662

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

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

F

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001757

C

Seeded from EcoCyc (v14.0)

complete

GO:0016773

phosphotransferase activity, alcohol group as acceptor

PMID:16889420[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0016787

hydrolase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000150

F

Seeded from EcoCyc (v14.0)

complete

GO:0016787

hydrolase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc (v14.0)

complete

GO:0033883

pyridoxal phosphatase activity

PMID:16990279[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0050308

sugar-phosphatase activity

PMID:16889420[6]

IDA: Inferred from Direct Assay

F

complete

GO:0016773

phosphotransferase activity, alcohol group as acceptor

PMID:16889420[6]

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[5]

IDA: Inferred from Direct Assay

F

Figure 1 and Table 2.

complete

GO:0016791

phosphatase activity

PMID:16990279[5]

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[5]

IDA: Inferred from Direct Assay

F

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

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

Protein

groL

PMID:16606699[7]

Experiment(s):EBI-1137896

Protein

moaA

PMID:16606699[7]

Experiment(s):EBI-1137896
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Notes

Localization

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

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 

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)

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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

146..235

PF00702 haloacid dehalogenase-like hydrolase

PMID:19920124[8]

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

Structures

<beststructure> gene=ybhA 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:16128734

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0002607

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P21829

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11239

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11239

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945372

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001217

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945372

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1221

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 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. ↑ 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 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
  6. ↑ 6.0 6.1 6.2 Saito, N et al. (2006) Metabolomics approach for enzyme discovery. J. Proteome Res. 5 1979-87 PubMed
  7. ↑ 7.0 7.1 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  8. ↑ Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

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