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talB: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

TalB

Synonyms

transaldolase B[1], B0008[2][1], YaaK[2][1], TalB[2][1]

Product description

transaldolase B[2][3];

Component of transaldolase B[2][3]

Transaldolase B[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:0016740

transferase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0808

F

Seeded from EcoCyc [5]

complete

GO:0008152

metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

P

Seeded from EcoCyc [5]

complete

GO:0006098

pentose-phosphate shunt

GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR004730
SP_KW:KW-0570
HAMAP:MF_00492

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001585

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0005737

cytoplasm

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR004730
SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [6]

complete

GO:0004801

transaldolase activity

GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR004730
EC:2.2.1.2
HAMAP:MF_00492

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0003824

catalytic activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013785

F

Seeded from EcoCyc [5]

complete

GO:0005739

mitochondrion

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [5]

complete

GO:0005829

cytosol

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [5]

complete

GO:0009052

pentose-phosphate shunt, non-oxidative branch

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0004801

transaldolase activity

PMID:7592346[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 11.1[3].

complete

GO:0005624

membrane_fraction

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc 12.5 [6]

GO:0004801

transaldolase_activity

PMID:7592346[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [6]


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

Partner TypePartnerNotesReferencesEvidence

Protein

Subunits of transaldolase B

could be indirect


Notes

Localization

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

CompartmentDescriptionEvidenceSourceNotes

Cytoplasm


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

MTDKLTSLRQ YTTVVADTGD IAAMKLYQPQ DATTNPSLIL NAAQIPEYRK LIDDAVAWAK
QQSNDRAQQI VDATDKLAVN IGLEILKLVP GRISTEVDAR LSYDTEASIA KAKRLIKLYN
DAGISNDRIL IKLASTWQGI RAAEQLEKEG INCNLTLLFS FAQARACAEA GVFLISPFVG
RILDWYKANT DKKEYAPAED PGVVSVSEIY QYYKEHGYET VVMGASFRNI GEILELAGCD
RLTIAPALLK ELAESEGAIE RKLSYTGEVK ARPARITESE FLWQHNQDPM AVDKLAEGIR
KFAIDQEKLE KMIGDLL
Length

317

Mol. Wt

35.22 kDa

pI

4.9 (calculated)

Extinction coefficient

39,880 - 40,255 (calc based on 12 Y, 4 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

Initiator Methionine

1

Removed

UniProt:P0A870

Modification Site

33

phosphorylation site at T33

probability less than 75%

PMID:17938405[9]

Modification Site

34

phosphorylation site at T34

probability less than 75%

PMID:17938405[9]

Modification Site

37

phosphorylation site at S37

probability greater than 75%

PMID:17938405[9]

Modification Site

226

phosphorylation site at S226

probability greater than 75%

PMID:17938405[9]


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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:TRANSALDOLB-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A870

PFAM (EcoliWiki Page)

PFAM:PF00923

RefSeq (EcoliWiki Page)

RefSeq:NP_414549


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 1.4 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 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 3.3 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 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. 6.0 6.1 6.2 6.3 6.4 6.5 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 Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed EcoliWiki page
  8. 8.0 8.1 Sprenger GA et al. (1995) Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains. J Bacteriol 177: 5930-6 PubMed EcoliWiki page
  9. 9.0 9.1 9.2 9.3 Macek B et al. (2007) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics PubMed EcoliWiki page

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