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Protein

Aconitate hydratase A

Gene

acnA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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

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. 2-methylcitrate dehydratase (prpD), Aconitate hydratase B (acnB), 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)DescriptionActionsGraphical viewLength
Metal bindingi435Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi501Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi504Iron-sulfur (4Fe-4S)By similarity1

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

Keywordsi

Molecular functionLyase, RNA-binding
Biological processTricarboxylic acid cycle
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:ACONITASE-MONOMER
MetaCyc:ACONITASE-MONOMER
BRENDAi4.2.1.3 2026
SABIO-RKiP25516
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11325 acnA

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000766612 – 891Aconitate hydratase AAdd BLAST890

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, 23 interactors
851065, 1 interactor
DIPiDIP-9043N
IntActiP25516, 13 interactors
STRINGi316385.ECDH10B_1393

Structurei

3D structure databases

ProteinModelPortaliP25516
SMRiP25516
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4107QM5 Bacteria
COG1048 LUCA
HOGENOMiHOG000025704
InParanoidiP25516
KOiK01681
OMAiMRIIPPG
PhylomeDBiP25516

Family and domain databases

Gene3Di3.20.19.10, 1 hit
3.30.499.10, 1 hit
InterProiView protein in InterPro
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR006249 Aconitase/IRP2
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR000573 AconitaseA/IPMdHydase_ssu_swvl
PANTHERiPTHR11670 PTHR11670, 1 hit
PfamiView protein in Pfam
PF00330 Aconitase, 1 hit
PF00694 Aconitase_C, 1 hit
PRINTSiPR00415 ACONITASE
SUPFAMiSSF53732 SSF53732, 1 hit
TIGRFAMsiTIGR01341 aconitase_1, 1 hit
PROSITEiView protein in PROSITE
PS00450 ACONITASE_1, 1 hit
PS01244 ACONITASE_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti522S → G in CAA42834 (PubMed:1541275).Curated1
Sequence conflicti522S → G in BAA14828 (PubMed:16738553).Curated1

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
PATRICifig|511145.12.peg.1327

Similar proteinsi

Entry informationi

Entry nameiACNA_ECOLI
AccessioniPrimary (citable) accession number: P25516
Secondary accession number(s): P78060, P78148
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 15, 2008
Last modified: March 28, 2018
This is version 155 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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