abgA:Gene Product(s)

From EcoliWiki
Jump to: navigation, search

{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>

Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
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

AbgA

Synonyms

predicted peptidase, aminobenzoyl-glutamate utilization protein[1], B1338[2][1], YdaJ[2][1], AbgA[2][1] , ECK1334, JW5205, ydaJ, b1338

Product description

protein with similarity to aminoacyl aminohydrolases[2][3]

Required for p-aminobenzoyl-glutamate utilization[4]

EC number (for enzymes)

<protect></protect>

Notes

Function

[back to top]


<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:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0006508

proteolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002933

P

Seeded from EcoCyc (v14.0)

complete

GO:0008237

metallopeptidase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002933

F

Seeded from EcoCyc (v14.0)

complete

GO:0016787

hydrolase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011650

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:0046983

protein dimerization activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011650

F

Seeded from EcoCyc (v14.0)

complete

GO:0071713

para-aminobenzoyl-glutamate hydrolase activity

PMID:17307853[5]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005737

cytoplasm

PMID:20190044[6]

IDA: Inferred from Direct Assay

C

complete

GO:0046657

folic acid catabolic process

PMID:9829935[7]

IGI: Inferred from Genetic Interaction

EcoliWiki:pabA


P

complete

GO:0046982

protein heterodimerization activity

PMID:20190044[6]

IPI: Inferred from Physical Interaction

EcoliWiki:abgB


F

complete

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

</protect>

Notes

Localization

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

Compartment Description Evidence Reference/Source Notes

<protect></protect>

Notes

Structure and Physical Properties

[back to top]


<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

MTGKVMESLN QFVNSLAPKL SHWRRDFHHY AESGWVEFRT ATLVAEELHQ LGYSLALGRE
VVNESSRMGL PDEFTLQREF ERARQQGALA QWIAAFEGGF TGIVATLDTG RPGPVMAFRV
DMDALDLSEE QDVSHRPYRD GFASCNAGMM HACGHDGHTA IGLGLAHTLK QFESGLHGVI
KLIFQPAEEG TRGARAMVDA GVVDDVDYFT AVHIGTGVPA GTVVCGSDNF MATTKFDAHF
TGTAAHAGAK PEDGHNALLA AAQATLALHA IAPHSEGASR VNVGVMQAGS GRNVVPASAL
LKVETRGASD VINQYVFDRA QQAIQGAATM YGVGVETRLM GAATASSPSP QWVAWLQSQA
AQVAGVNQAI ERVEAPAGSE DATLMMARVQ QHQGQASYVV FGTQLAAGHH NEKFDFDEQV
LAIAVETLAR TALNFPWTRG I
Length

441

Mol. Wt

47.102 kDa

pI

5.8 (calculated)

Extinction coefficient

43,430 - 43,805 (calc based on 7 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.

Type Residues Description Notes References

Domain

112..429

PF01546 Peptidase family M20/M25/M40

PMID:19920124[8]

Domain

226..326

PF07687 Peptidase dimerisation domain

PMID:19920124[8]

<motif_map/>

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

Structures

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

Models

View models at:

</protect>

Structure figures

<protect>

</protect>

Notes

Gene Product Resources

[back to top]


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

Resource type Source Notes/Reference

<protect></protect>

Notes

Accessions in Other Databases

[back to top]


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

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:90111252

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:945742

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0004493

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P77357

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:G6670

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG13352

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:945742

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120003265

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB3135

Escherichia coli str. K-12 substr. MG1655

<protect></protect>

Notes

Links

[back to top]




References

[back to top]


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

  1. 1.0 1.1 1.2 1.3 1.4 1.5 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. Carter, EL et al. (2007) Escherichia coli abg genes enable uptake and cleavage of the folate catabolite p-aminobenzoyl-glutamate. J. Bacteriol. 189 3329-34 PubMed
  6. 6.0 6.1 Green, JM et al. (2010) Purification and characterization of the folate catabolic enzyme p-aminobenzoyl-glutamate hydrolase from Escherichia coli. J. Bacteriol. 192 2407-13 PubMed
  7. Hussein, MJ et al. (1998) Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli. J. Bacteriol. 180 6260-8 PubMed
  8. 8.0 8.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

[back to top]