acnA:Gene Product(s) - EcoliWiki
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acnA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

AcnA

Synonyms

aconitate hydratase 1[1], B1276[2][1], Acn[2][1], AcnA[2][1]

Product description

ACONITASE[2][3]

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.

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0006099

tricarboxylic acid cycle

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0816

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0005506

iron ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0003994

aconitate hydratase activity

GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:4.2.1.3

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0016829

lyase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0456

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0008152

metabolic process

GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000573
InterPro:IPR001030
InterPro:IPR006249
InterPro:IPR015928
InterPro:IPR015931
InterPro:IPR015932
InterPro:IPR015934
InterPro:IPR015937

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GO_REF:0000002
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR006249
SP_KW:KW-0004

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0051536

iron-sulfur cluster binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0411

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0005515

protein binding

PMID:16606699[5]

IPI: Inferred from Physical Interaction

UniProtKB:P18843

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006979

response to oxidative stress

PMID:9421904[6]

IEP: Inferred from Expression Pattern

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0043556

regulation of translation in response to oxidative stress

PMID:10589714[7]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0003994

aconitate hydratase activity

PMID:1838390[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [4]

complete

GO:0006099

tricarboxylic acid cycle

PMID:13152052[9]

IDA: Inferred from Direct Assay

P

Seeded from EcoCyc 11.1[3].

complete

GO:0009061

anaerobic respiration

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006979

response to oxidative stress

PMID:9421904[6]

IEP: Inferred from Expression Pattern

P

Seeded from EcoCyc 11.1[3].

complete

GO:0003994

aconitate hydratase activity

PMID:1838390[8]

IDA: Inferred from Direct Assay

F

complete

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Interactions

Partner TypePartnerNotesReferences
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Notes

Localization

CompartmentDescriptionEvidenceNotes
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Notes

Structure and Physical Properties

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Physical Properties

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
Mol. Wt

97.68 kDa (calc) [2]

pI
Extinction coefficient

114710 - 115585 (calc based on 29 Y, 13 W, and 7 C residues)

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Domains/Motifs/Modification Sites

TypeResiduesDescriptionNotes
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Structure

Structures
  • Representative homolog:
    2IPY|A (Oryctolagus cuniculus)
    33-888 of 891 residues (E-value: 1.1e-239) (Percent Identity: 53.29)
  • View all other structures.
Models

View models at:

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Notes

Gene Product Resources

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Resource typeSourceNotes/Reference
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Notes

Accessions in Other Databases

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DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:ACONITASE-MONOMER

UniProt (EcoliWiki Page)

UniProt:P25516

PFAM (EcoliWiki Page)

PFAM:PF00330

RefSeq (EcoliWiki Page)

RefSeq:NP_415792

ModBase (EcoliWiki Page)

ModBase:P25516


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Notes

Links

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NameURLComments
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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 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. 4.00 4.01 4.02 4.03 4.04 4.05 4.06 4.07 4.08 4.09 4.10 4.11 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
  6. 6.0 6.1 Cunningham L et al. (1997) Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli. Microbiology 143 ( Pt 12): 3795-805 PubMed EcoliWiki page
  7. Tang Y & Guest JR (1999) Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases. Microbiology 145 ( Pt 11): 3069-79 PubMed EcoliWiki page
  8. 8.0 8.1 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 EcoliWiki page
  9. SWIM HE & KRAMPITZ LO (1954) Acetic acid oxidation by Escherichia coli; evidence for the occurrence of a tricarboxylic acid cycle. J Bacteriol 67: 419-25 PubMed EcoliWiki page


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