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P36683 (ACON2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
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 2
Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
2-methylisocitrate dehydratase
EC=4.2.1.99
Citrate hydro-lyase
Gene names
Name:acnB
Synonyms:yacI, yacJ
Ordered Locus Names:b0118, JW0114
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate.

Catalytic activity

Citrate = isocitrate. Ref.6 Ref.7

(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O. Ref.6 Ref.7

Cofactor

Binds 1 4Fe-4S cluster per subunit.

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=11 mM for citrate Ref.6 Ref.7

KM=0.016 mM for cis-aconitate

KM=0.051 mM for isocitrate (using 0.01-0.8 mM substrate)

KM=19.7 mM for isocitrate (using 0.8-40 mM substrate)

KM=0.21 mM for (2R,3S)-2-methylisocitrate

Vmax=23.8 µmol/min/mg enzyme with citrate as substrate

Vmax=39.1 µmol/min/mg enzyme with cis-aconitate as substrate

Vmax=5.92 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate

Vmax=57.8 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

Chain1 – 865865Aconitate hydratase 2
PRO_0000076675

Regions

Region244 – 2463Substrate binding
Region414 – 4163Substrate binding

Sites

Metal binding7101Iron-sulfur (4Fe-4S)
Metal binding7691Iron-sulfur (4Fe-4S)
Metal binding7721Iron-sulfur (4Fe-4S)
Binding site1911Substrate
Binding site4981Substrate
Binding site7911Substrate
Binding site7961Substrate

Secondary structure

1 ........................................................................................................................................... 865
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36683 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: FEC8AA5D2A9DD2BD

FASTA86593,498
        10         20         30         40         50         60 
MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA 

        70         80         90        100        110        120 
AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS 

       130        140        150        160        170        180 
HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD 

       190        200        210        220        230        240 
DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV 

       250        260        270        280        290        300 
GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN 

       310        320        330        340        350        360 
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA 

       370        380        390        400        410        420 
LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM 

       430        440        450        460        470        480 
TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH 

       490        500        510        520        530        540 
SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM 

       550        560        570        580        590        600 
QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA 

       610        620        630        640        650        660 
ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA 

       670        680        690        700        710        720 
DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA 

       730        740        750        760        770        780 
GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA 

       790        800        810        820        830        840 
DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT 

       850        860 
YRYLNFNQLS QYTEKADGVI FQTAV

« Hide

References

« Hide 'large scale' references
[1]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"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.
[3]"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], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The second aconitase (AcnB) of Escherichia coli."
Bradbury A.J., Gruer M.J., Rudd K.E., Guest J.R.
Microbiology 142:389-400(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131, PROTEIN SEQUENCE OF 1-11, CHARACTERIZATION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[6]"Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase."
Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.
Eur. J. Biochem. 269:6184-6194(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15, CATALYTIC ACTIVITY AS 2-METHYLISOCITRATE LYASE, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[7]"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: PROTEIN SEQUENCE OF 568-663, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY.
[8]"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: CHARACTERIZATION.
[9]"E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition."
Williams C.H. Jr., Stillman T.J., Barynin V.V., Sedelnikova S.E., Tang Y., Green J., Guest J.R., Artymiuk P.J.
Nat. Struct. Biol. 9:447-452(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR AND ACONITATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U00096 Genomic DNA. Translation: AAC73229.1.
AP009048 Genomic DNA. Translation: BAB96692.2.
U41560 Genomic DNA. Translation: AAC43710.1.
PIRF64734.
RefSeqNP_414660.1. NC_000913.2.
YP_488421.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L5JX-ray2.40A/B1-865[»]
ProteinModelPortalP36683.
SMRP36683. Positions 1-862.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9044N.
IntActP36683. 15 interactions.
STRING511145.b0118.

PTM databases

PhosSiteP0809366.

2D gel databases

SWISS-2DPAGEP36683.

Proteomic databases

PaxDbP36683.
PRIDEP36683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73229; AAC73229; b0118.
BAB96692; BAB96692; BAB96692.
GeneID12932908.
944864.
KEGGecj:Y75_p0115.
eco:b0118.
PATRIC32115337. VBIEscCol129921_0120.

Organism-specific databases

EchoBASEEB2222.
EcoGeneEG12316. acnB.

Phylogenomic databases

eggNOGCOG1049.
HOGENOMHOG000205991.
KOK01682.
OMANVFNGRI.
ProtClustDBPRK09238.

Enzyme and pathway databases

BioCycEcoCyc:ACONITATEDEHYDRB-MONOMER.
ECOL316407:JW0114-MONOMER.
MetaCyc:ACONITATEDEHYDRB-MONOMER.
BRENDA4.2.1.3. 2026.
SABIO-RKP36683.
UniPathwayUPA00223; UER00718.

Gene expression databases

GenevestigatorP36683.

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.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR004406. Aconitase_B_bac.
IPR015930. Aconitase_B_FeS-bd_bac.
IPR015933. Aconitase_B_HEAT-like_bac.
IPR015929. Aconitase_B_N_bac.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF3. PTHR11670:SF3. 1 hit.
PfamPF00330. Aconitase. 2 hits.
PF06434. Aconitase_2_N. 1 hit.
PF11791. Aconitase_B_N. 1 hit.
[Graphical view]
PIRSFPIRSF036687. AcnB. 1 hit.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF74778. Aconitase_B_HEAT-like_bac. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR00117. acnB. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36683.

Entry information

Entry nameACON2_ECOLI
AccessionPrimary (citable) accession number: P36683
Secondary accession number(s): P36648, P75652, Q59382
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 127 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents