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P25516 (ACON1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aconitate hydratase 1

Short name=Aconitase 1
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase 1
Gene names
Name:acnA
Synonyms:acn
Ordered Locus Names:b1276, JW1268
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length891 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. May have an iron-responsive regulatory function.

Catalytic activity

Citrate = isocitrate. Ref.6

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.

Subunit structure

Monomer.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.16 mM for citrate Ref.6

KM=0.058 mM for cis-aconitate

KM=0.014 mM for isocitrate (using 0.01-0.8 mM substrate)

KM=1.77 mM for isocitrate (using 0.8-40 mM substrate)

Vmax=6.13 µmol/min/mg enzyme with citrate as substrate

Vmax=14.5 µmol/min/mg enzyme with cis-aconitate as substrate

Vmax=3.57 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate

Vmax=14.7 µmol/min/mg enzyme using 0.8-40 mM isocitrate as substrate

pH dependence:

Optimum pH is 7.4.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 891890Aconitate hydratase 1
PRO_0000076661

Sites

Metal binding4351Iron-sulfur (4Fe-4S) By similarity
Metal binding5011Iron-sulfur (4Fe-4S) By similarity
Metal binding5041Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict5221S → G in CAA42834. Ref.1
Sequence conflict5221S → G in BAA14828. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P25516 [UniParc].

Last modified January 15, 2008. Version 3.
Checksum: EB47E5B3C3F9C56C

FASTA89197,677
        10         20         30         40         50         60 
MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL RWQDGNSVTE 

        70         80         90        100        110        120 
EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL AAMREAVKRL GGDTAKVNPL 

       130        140        150        160        170        180 
SPVDLVIDHS VTVDRFGDDE AFEENVRLEM ERNHERYVFL KWGKQAFSRF SVVPPGTGIC 

       190        200        210        220        230        240 
HQVNLEYLGK AVWSELQDGE WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ 

       250        260        270        280        290        300 
PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR 

       310        320        330        340        350        360 
ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW RNPGDEPIFT 

       370        380        390        400        410        420 
STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE VNATHKDRQP VDYVMNGHQY 

       430        440        450        460        470        480 
QLPDGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVTLGLK RQPWVKASLA PGSKVVSDYL 

       490        500        510        520        530        540 
AKAKLTPYLD ELGFNLVGYG CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI 

       550        560        570        580        590        600 
HPLVKTNWLA SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ 

       610        620        630        640        650        660 
VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ ATPAPVEDIH 

       670        680        690        700        710        720 
GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER KDFNSYGSRR GNHEVMMRGT 

       730        740        750        760        770        780 
FANIRIRNEM VPGVEGGMTR HLPDSDVVSI YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW 

       790        800        810        820        830        840 
AAKGPRLLGI RVVIAESFER IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN 

       850        860        870        880        890 
LQPGATVPVT LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K 

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
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.
[6]"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: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60293 Genomic DNA. Translation: CAA42834.1.
U00096 Genomic DNA. Translation: AAC74358.1.
AP009048 Genomic DNA. Translation: BAA14828.1.
PIRG64875.
RefSeqNP_415792.1. NC_000913.2.
YP_489544.1. NC_007779.1.

3D structure databases

ProteinModelPortalP25516.
SMRP25516. Positions 37-891.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9043N.
IntActP25516. 4 interactions.
MINTMINT-1249275.
STRING511145.b1276.

Proteomic databases

PaxDbP25516.
PRIDEP25516.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74358; AAC74358; b1276.
BAA14828; BAA14828; BAA14828.
GeneID12931140.
946724.
KEGGecj:Y75_p1251.
eco:b1276.
PATRIC32117814. VBIEscCol129921_1327.

Organism-specific databases

EchoBASEEB1301.
EcoGeneEG11325. acnA.

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000025704.
KOK01681.
OMAYSKAQGM.
ProtClustDBPRK09277.

Enzyme and pathway databases

BioCycEcoCyc:ACONITASE-MONOMER.
ECOL316407:JW1268-MONOMER.
MetaCyc:ACONITASE-MONOMER.
UniPathwayUPA00223; UER00718.

Gene expression databases

GenevestigatorP25516.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_prot_2.
IPR015934. Aconitase/Fe_reg_prot_2/AcnD.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF1. PTHR11670:SF1. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01341. aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACON1_ECOLI
AccessionPrimary (citable) accession number: P25516
Secondary accession number(s): P78060, P78148
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 15, 2008
Last modified: May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families