acnB: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

AcnB

Synonyms

bifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase[1], B0118[2][1], YacI[2][1], YacJ[2][1], AcnB[2][1] , ECK0117, JW0114, yacI, yacJ, b0118

Product description

Aconitase B; 2-methylaconitate hydratase; apo-enzyme binds mRNA for negative translational autoregulation; iron-sulfur cluster; monomeric[3]

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
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0003994

aconitate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004406

F

Seeded from EcoCyc (v14.0)

complete

GO:0003994

aconitate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015929

F

Seeded from EcoCyc (v14.0)

complete

GO:0003994

aconitate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015930

F

Seeded from EcoCyc (v14.0)

complete

GO:0003994

aconitate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015933

F

Seeded from EcoCyc (v14.0)

complete

GO:0003994

aconitate hydratase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:4.2.1.3

F

Seeded from EcoCyc (v14.0)

complete

GO:0003994

aconitate hydratase activity

PMID:8932712[4]

IDA: Inferred from Direct Assay

F

complete

GO:0005506

iron ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004406

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015929

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015933

F

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004406

P

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015929

P

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015930

P

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015933

P

Seeded from EcoCyc (v14.0)

complete

GO:0006099

tricarboxylic acid cycle

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0816

P

Seeded from EcoCyc (v14.0)

complete

GO:0046872

metal ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004406

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR015930

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0004

F

Seeded from EcoCyc (v14.0)

complete

GO:0006097

glyoxylate cycle

PMID:10589714[5]

NAS: Non-traceable Author Statement

P

complete

GO:0006099

tricarboxylic acid cycle

PMID:10589714[5]

NAS: Non-traceable Author Statement

P

complete

GO:0003729

mRNA binding

PMID:10589714[5]

IDA: Inferred from Direct Assay

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

Protein

speD

PMID:16606699[6]

Experiment(s):EBI-1135623, EBI-1135640

Protein

zwf

PMID:16606699[6]

Experiment(s):EBI-1135623

Protein

ulaB

PMID:16606699[6]

Experiment(s):EBI-1135623

Protein

sbcC

PMID:16606699[6]

Experiment(s):EBI-1135623

Protein

groL

PMID:16606699[6]

Experiment(s):EBI-1135623

Protein

groS

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

dapB

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

gatA

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

gcvP

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

gabD

PMID:19402753[7]

LCMS(ID Probability):99.6

Protein

php

PMID:19402753[7]

LCMS(ID Probability):99.4

</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

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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

MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA
AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS
HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD
DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV
GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA
LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM
TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH
SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM
QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA
DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA
GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA
DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT
YRYLNFNQLS QYTEKADGVI FQTAV
Length

865

Mol. Wt

93.5 kDa

pI

5.2 (calculated)

Extinction coefficient

75,290 - 76,540 (calc based on 21 Y, 8 W, and 10 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

Modification Site

242

phosphorylation site at T242

probability less than 75%

PMID:17938405[8]

Modification Site

622

phosphorylation site at S622

probability greater than 75%

PMID:17938405[8]

Modification Site

245

phosphorylation site at S245

probability less than 75%

PMID:17938405[8]

Modification Site

242

phosphorylation site at T242

probability less than 75%

PMID:17938405[8]

Domain

464..701

PF00330 Aconitase family (aconitate hydratase)

PMID:19920124[9]

Domain

695..818

PF00330 Aconitase family (aconitate hydratase)

PMID:19920124[9]

Domain

168..382

PF06434 Aconitate hydratase 2 N-terminus

PMID:19920124[9]

Domain

4..156

PF11791 Aconitate B N-terminal domain

PMID:19920124[9]

<motif_map/>

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

Structures

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

Models

View models at:

</protect>

Structure figures

<protect>

</protect>

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

<protect></protect>

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:16128111

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:944864

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000411

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P36683

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG12316

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG12316

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:944864

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120002193

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB2222

Escherichia coli str. K-12 substr. MG1655

<protect></protect>

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 1.5 1.6 1.7 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. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  4. Bradbury, AJ et al. (1996) The second aconitase (AcnB) of Escherichia coli. Microbiology (Reading, Engl.) 142 ( Pt 2) 389-400 PubMed
  5. 5.0 5.1 5.2 Tang, Y & Guest, JR (1999) Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology (Reading, Engl.) 145 ( Pt 11) 3069-79 PubMed
  6. 6.0 6.1 6.2 6.3 6.4 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  7. 7.0 7.1 7.2 7.3 7.4 7.5 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  8. 8.0 8.1 8.2 8.3 Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed
  9. 9.0 9.1 9.2 9.3 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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