rhmA:Gene Product(s)

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

YfaU product

Synonyms

predicted 2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolase product[1], B2245 product[2][1], YfaU product[2][1]

Product description

predicted aldolase[2][3] metal-dependent class II aldolase belonging to the pyruvate/enolpyruvate binding (�/R)8 barrel superfamily.[4], Genomic context suggested a 2-dehydro-3-deoxy sugar aldolase function rather than the 4-hydroxy-2-ketoheptane- 1,7-dioate aldolase function as annotated in the databases based on homology with the related HpcH. Functional assignment of YfaW as a L-rhamnonate dehydratase suggested 2-dehydro-3-deoxy-L-rhamnonate is the physiological substrate of YfaU, and enzyme kinetic measurements support this assignment.

EC number (for enzymes)
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Notes

Function

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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(s) Evidence Code with/from Aspect Notes Status
GO:0003824

catalytic_activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015813

F

Seeded from EcoCyc 12.5 [5]

GO:0006725

aromatic_compound_metabolism

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005000

P

Seeded from EcoCyc 12.5 [5]

GO:0016829

lyase_activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0456

F

Seeded from EcoCyc 12.5 [5]

GO:0008152

metabolic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0016830

carbon-carbon_lyase_activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005000

F

Seeded from EcoCyc 12.5 [5]


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Interactions

Partner Type Partner Notes
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Notes

Localization

Compartment Description Evidence Notes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MNALLSNPFK ERLRKGEVQI GLWLSSTTAY MAEIAATSGY DWLLIDGEHA PNTIQDLYHQ
LQAVAPYASQ PVIRPVEGSK PLIKQVLDIG AQTLLIPMVD TAEQARQVVS ATRYPPYGER
GVGASVARAA RWGRIENYMA QVNDSLCLLV QVESKTALDN LDEILDVEGI DGVFIGPADL
SASLGYPDNA GHPEVQRIIE TSIRRIRAAG KAAGFLAVAP DMAQQCLAWG ANFVAVGVDT
MLYSDALDQR LAMFKSGKNG PRIKGSY
Mol. Wt

28.92 kDa (calc) [2]

pI
Extinction coefficient

36900 - 37150 (calc based on 10 Y, 4 W, and 2 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes
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Structure

Structures Models

1.39 A structure of apo-YfaU and the Mg2+-pyruvate product complex [4]


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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:G7158-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:P76469

UniProt (EcoliWiki Page)

UniProt:P76469

PFAM (EcoliWiki Page)

PFAM:PF03328

RefSeq (EcoliWiki Page)

RefSeq:NP_416748

ModBase (EcoliWiki Page)

ModBase:P76469

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Notes

Links

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Name URL Comments
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References

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  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 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. ↑ 4.0 4.1 Rea, D et al. (2008) Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12. Biochemistry 47 9955-65 PubMed
  5. ↑ 5.0 5.1 5.2 5.3 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7


Categories

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