acnA: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

AcnA

Synonyms

aconitate hydratase 1[1], B1276[2][1], Acn[2][1], AcnA[2][1] , acn, ECK1271, JW1268, b1276

Product description

Aconitase A, stationary phase induced; iron-sulfur cluster; apo-enzyme binds mRNA for negative translational autoregulation; negatively regulated by ryhB RNA as part of indirect positive regulation by Fur[3]

EC number (for enzymes)

4.2.1.3[1]

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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

PMID:1838390[4]

IDA: Inferred from Direct Assay

F

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: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: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:0051539

4 iron, 4 sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006249

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:0003729

mRNA binding

PMID:10589714[5]

IDA: Inferred from Direct Assay

F

complete

GO:0006099

tricarboxylic acid cycle

PMID:10589714[5]

NAS: Non-traceable Author Statement

P

complete

GO:0006097

glyoxylate cycle

PMID:10589714[5]

NAS: Non-traceable Author Statement

P

complete

GO:0005506

iron ion binding

PMID:12486059[6]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0046872

metal ion binding

PMID:12486059[6]

IDA: Inferred from Direct Assay

F

complete

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:12486059[6]

IDA: Inferred from Direct Assay

F

complete

GO:0006979

response to oxidative stress

PMID:12486059[6]

IDA: Inferred from Direct Assay

P

complete

GO:0009061

anaerobic respiration

PMID:12486059[6]

IDA: Inferred from Direct Assay

P

complete

GO:0005737

cytoplasm

PMID:12486059[6]

IDA: Inferred from Direct Assay

C

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

nadE

PMID:16606699[7]

Experiment(s):EBI-1139437

Protein

gadB

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

rplS

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

rplX

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

glgP

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

rpsA

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

yhbY

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

rpmF

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

rho

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

tig

PMID:19402753[8]

LCMS(ID Probability):99.6

Protein

csrA

PMID:19402753[8]

LCMS(ID Probability):99.6

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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

MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL RWQDGNSVTE
EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL AAMREAVKRL GGDTAKVNPL
SPVDLVIDHS VTVDRFGDDE AFEENVRLEM ERNHERYVFL KWGKQAFSRF SVVPPGTGIC
HQVNLEYLGK AVWSELQDGE WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR
ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW RNPGDEPIFT
STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE VNATHKDRQP VDYVMNGHQY
QLPDGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVTLGLK RQPWVKASLA PGSKVVSDYL
AKAKLTPYLD ELGFNLVGYG CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI
HPLVKTNWLA SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ
VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ ATPAPVEDIH
GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER KDFNSYGSRR GNHEVMMRGT
FANIRIRNEM VPGVEGGMTR HLPDSDVVSI YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW
AAKGPRLLGI RVVIAESFER IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN
LQPGATVPVT LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K
Length

891

Mol. Wt

97.678 kDa

pI

5.8 (calculated)

Extinction coefficient

114,710 - 115,585 (calc based on 29 Y, 13 W, and 7 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

Initiator Methionine

1

Removed

UniProt:P25516

Domain

57..562

PF00330 Aconitase family (aconitate hydratase)

PMID:19920124[9]

Domain

689..819

PF00694 Aconitase C-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=acnA 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:16129237

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946724

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0004283

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P25516

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG11325

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG11325

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946724

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001296

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB1301

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 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 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. Prodromou, C et al. (1991) The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn). J. Gen. Microbiol. 137 2505-15 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 6.5 Varghese, S et al. (2003) Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J. Bacteriol. 185 221-30 PubMed
  7. Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  8. 8.0 8.1 8.2 8.3 8.4 8.5 8.6 8.7 8.8 8.9 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  9. 9.0 9.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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