Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aconitate hydratase A

Gene

acnA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3' UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript.6 Publications

Catalytic activityi

Citrate = isocitrate.1 Publication

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit.2 Publications

Kineticsi

  1. KM=1.16 mM for citrate1 Publication
  2. KM=0.058 mM for cis-aconitate1 Publication
  3. KM=0.014 mM for isocitrate (using 0.01-0.8 mM substrate)1 Publication
  4. KM=1.77 mM for isocitrate (using 0.8-40 mM substrate)1 Publication
  1. Vmax=6.13 µmol/min/mg enzyme with citrate as substrate1 Publication
  2. Vmax=14.5 µmol/min/mg enzyme with cis-aconitate as substrate1 Publication
  3. Vmax=3.57 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate1 Publication
  4. Vmax=14.7 µmol/min/mg enzyme using 0.8-40 mM isocitrate as substrate1 Publication

pH dependencei

Optimum pH is 7.4. It retains a high specific activity over a broad pH range.1 Publication

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.Curated
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase (gltA)
  2. Aconitate hydratase B (acnB), 2-methylcitrate dehydratase (prpD), Aconitate hydratase A (acnA), 2-methylcitrate synthase (prpC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi435 – 4351Iron-sulfur (4Fe-4S)By similarity
Metal bindingi501 – 5011Iron-sulfur (4Fe-4S)By similarity
Metal bindingi504 – 5041Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoliWiki
  • aconitate hydratase activity Source: EcoliWiki
  • iron ion binding Source: EcoliWiki
  • metal ion binding Source: EcoliWiki
  • mRNA 3'-UTR binding Source: EcoCyc
  • mRNA binding Source: EcoliWiki

GO - Biological processi

  • anaerobic respiration Source: EcoliWiki
  • glyoxylate cycle Source: EcoliWiki
  • response to oxidative stress Source: EcoliWiki
  • tricarboxylic acid cycle Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACONITASE-MONOMER.
ECOL316407:JW1268-MONOMER.
MetaCyc:ACONITASE-MONOMER.
BRENDAi4.2.1.3. 2026.
UniPathwayiUPA00223; UER00718.

Names & Taxonomyi

Protein namesi
Recommended name:
Aconitate hydratase A1 Publication (EC:4.2.1.31 Publication)
Short name:
ACN1 Publication
Short name:
Aconitase1 Publication
Alternative name(s):
Iron-responsive protein-like1 Publication
Short name:
IRP-like1 Publication
RNA-binding protein1 Publication
Stationary phase enzyme1 Publication
Gene namesi
Name:acnA1 Publication
Synonyms:acn
Ordered Locus Names:b1276, JW1268
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11325. acnA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are more sensitive to peroxide stress. The acnAB double mutant does not grow on unsupplemented glucose minimal medium and does not respond under aerobic conditions to glutamate. The acnAB double mutant retains a low but significant aconitase activity.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 891890Aconitate hydratase APRO_0000076661Add
BLAST

Proteomic databases

EPDiP25516.
PaxDbiP25516.
PRIDEiP25516.

Expressioni

Inductioni

Induced upon entry into stationary phase by iron, oxidative and salt stress under aerobic conditions. AcnA is subject to CRP-mediated catabolite repression and ArcA-mediated anaerobic repression. AcnA is negatively regulated by ryhB RNA.5 Publications

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4260134. 11 interactions.
851065. 1 interaction.
DIPiDIP-9043N.
IntActiP25516. 5 interactions.
MINTiMINT-1249275.
STRINGi511145.b1276.

Structurei

3D structure databases

ProteinModelPortaliP25516.
SMRiP25516. Positions 37-891.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4107QM5. Bacteria.
COG1048. LUCA.
HOGENOMiHOG000025704.
InParanoidiP25516.
KOiK01681.
OMAiENLAKWG.
OrthoDBiEOG67DPHM.
PhylomeDBiP25516.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006249. Aconitase/IRP2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 4 hits.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25516-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL
60 70 80 90 100
RWQDGNSVTE EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL
110 120 130 140 150
AAMREAVKRL GGDTAKVNPL SPVDLVIDHS VTVDRFGDDE AFEENVRLEM
160 170 180 190 200
ERNHERYVFL KWGKQAFSRF SVVPPGTGIC HQVNLEYLGK AVWSELQDGE
210 220 230 240 250
WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ PVSMLIPDVV
260 270 280 290 300
GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR
310 320 330 340 350
ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW
360 370 380 390 400
RNPGDEPIFT STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE
410 420 430 440 450
VNATHKDRQP VDYVMNGHQY QLPDGAVVIA AITSCTNTSN PSVLMAAGLL
460 470 480 490 500
AKKAVTLGLK RQPWVKASLA PGSKVVSDYL AKAKLTPYLD ELGFNLVGYG
510 520 530 540 550
CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI HPLVKTNWLA
560 570 580 590 600
SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ
610 620 630 640 650
VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ
660 670 680 690 700
ATPAPVEDIH GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER
710 720 730 740 750
KDFNSYGSRR GNHEVMMRGT FANIRIRNEM VPGVEGGMTR HLPDSDVVSI
760 770 780 790 800
YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW AAKGPRLLGI RVVIAESFER
810 820 830 840 850
IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN LQPGATVPVT
860 870 880 890
LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K
Length:891
Mass (Da):97,677
Last modified:January 15, 2008 - v3
Checksum:iEB47E5B3C3F9C56C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti522 – 5221S → G in CAA42834 (PubMed:1541275).Curated
Sequence conflicti522 – 5221S → G in BAA14828 (PubMed:16738553).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60293 Genomic DNA. Translation: CAA42834.1.
U00096 Genomic DNA. Translation: AAC74358.1.
AP009048 Genomic DNA. Translation: BAA14828.1.
PIRiG64875.
RefSeqiNP_415792.1. NC_000913.3.
WP_000099535.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74358; AAC74358; b1276.
BAA14828; BAA14828; BAA14828.
GeneIDi946724.
KEGGiecj:JW1268.
eco:b1276.
PATRICi32117814. VBIEscCol129921_1327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60293 Genomic DNA. Translation: CAA42834.1.
U00096 Genomic DNA. Translation: AAC74358.1.
AP009048 Genomic DNA. Translation: BAA14828.1.
PIRiG64875.
RefSeqiNP_415792.1. NC_000913.3.
WP_000099535.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP25516.
SMRiP25516. Positions 37-891.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260134. 11 interactions.
851065. 1 interaction.
DIPiDIP-9043N.
IntActiP25516. 5 interactions.
MINTiMINT-1249275.
STRINGi511145.b1276.

Proteomic databases

EPDiP25516.
PaxDbiP25516.
PRIDEiP25516.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74358; AAC74358; b1276.
BAA14828; BAA14828; BAA14828.
GeneIDi946724.
KEGGiecj:JW1268.
eco:b1276.
PATRICi32117814. VBIEscCol129921_1327.

Organism-specific databases

EchoBASEiEB1301.
EcoGeneiEG11325. acnA.

Phylogenomic databases

eggNOGiENOG4107QM5. Bacteria.
COG1048. LUCA.
HOGENOMiHOG000025704.
InParanoidiP25516.
KOiK01681.
OMAiENLAKWG.
OrthoDBiEOG67DPHM.
PhylomeDBiP25516.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
BioCyciEcoCyc:ACONITASE-MONOMER.
ECOL316407:JW1268-MONOMER.
MetaCyc:ACONITASE-MONOMER.
BRENDAi4.2.1.3. 2026.

Miscellaneous databases

PROiP25516.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006249. Aconitase/IRP2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 4 hits.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases."
    Prodromou C., Artymiuk P.J., Guest J.R.
    Eur. J. Biochem. 204:599-609(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn)."
    Prodromou C., Haynes M.J., Guest J.R.
    J. Gen. Microbiol. 137:2505-2515(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19, FUNCTION, SUBUNIT.
  6. "Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli."
    Gruer M.J., Guest J.R.
    Microbiology 140:2531-2541(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DISRUPTION PHENOTYPE.
  7. "Spectroscopic characterisation of an aconitase (AcnA) of Escherichia coli."
    Bennett B., Gruer M.J., Guest J.R., Thomson A.J.
    Eur. J. Biochem. 233:317-326(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  8. "Construction and properties of aconitase mutants of Escherichia coli."
    Gruer M.J., Bradbury A.J., Guest J.R.
    Microbiology 143:1837-1846(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Transcriptional regulation of the aconitase genes (acnA and acnB) of Escherichia coli."
    Cunningham L., Gruer M.J., Guest J.R.
    Microbiology 143:3795-3805(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  10. "Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)."
    Jordan P.A., Tang Y., Bradbury A.J., Thomson A.J., Guest J.R.
    Biochem. J. 344:739-746(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY, COFACTOR.
  11. "Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases."
    Tang Y., Guest J.R.
    Microbiology 145:3069-3079(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A RNA-BINDING PROTEIN.
  12. "Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression."
    Tang Y., Quail M.A., Artymiuk P.J., Guest J.R., Green J.
    Microbiology 148:1027-1037(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli."
    Masse E., Gottesman S.
    Proc. Natl. Acad. Sci. U.S.A. 99:4620-4625(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion."
    Varghese S., Tang Y., Imlay J.A.
    J. Bacteriol. 185:221-230(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  15. "Quantitative and kinetic study of oxidative stress regulons using green fluorescent protein."
    Lu C., Albano C.R., Bentley W.E., Rao G.
    Biotechnol. Bioeng. 89:574-587(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  16. "Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli."
    Weber A., Kogl S.A., Jung K.
    J. Bacteriol. 188:7165-7175(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiACNA_ECOLI
AccessioniPrimary (citable) accession number: P25516
Secondary accession number(s): P78060, P78148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 15, 2008
Last modified: March 16, 2016
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The AcnA activity over a broad pH range might be a useful adaptation for specifically expression in the stationary phase, where the intracellular pH may vary over a wider range. AcnA is resistant to oxidation in vivo.2 Publications

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.