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P20004 (ACON_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 128. 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, mitochondrial

Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
Name:ACO2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length780 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.

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit. Binding of a 3Fe-4S cluster leads to an inactive enzyme.

Pathway

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

Subunit structure

Monomer.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Ref.3
Chain28 – 780753Aconitate hydratase, mitochondrial
PRO_0000000540

Regions

Region192 – 1943Substrate binding
Region670 – 6712Substrate binding

Sites

Metal binding3851Iron-sulfur (4Fe-4S) Ref.3
Metal binding4481Iron-sulfur (4Fe-4S) Ref.3
Metal binding4511Iron-sulfur (4Fe-4S) Ref.3
Binding site991Substrate
Binding site4741Substrate
Binding site4791Substrate
Binding site6071Substrate

Amino acid modifications

Modified residue281Pyrrolidone carboxylic acid
Modified residue311N6-succinyllysine By similarity
Modified residue501N6-acetyllysine; alternate By similarity
Modified residue501N6-succinyllysine; alternate By similarity
Modified residue1381N6-acetyllysine; alternate By similarity
Modified residue1381N6-succinyllysine; alternate By similarity
Modified residue1441N6-acetyllysine; alternate By similarity
Modified residue1441N6-succinyllysine; alternate By similarity
Modified residue2331N6-acetyllysine; alternate By similarity
Modified residue2331N6-succinyllysine; alternate By similarity
Modified residue4111N6-succinyllysine By similarity
Modified residue5171N6-acetyllysine; alternate By similarity
Modified residue5171N6-succinyllysine; alternate By similarity
Modified residue5231N6-acetyllysine; alternate By similarity
Modified residue5231N6-succinyllysine; alternate By similarity
Modified residue5491N6-succinyllysine By similarity
Modified residue5591Phosphoserine By similarity
Modified residue5731N6-acetyllysine; alternate By similarity
Modified residue5731N6-succinyllysine; alternate By similarity
Modified residue5911N6-succinyllysine By similarity
Modified residue6051N6-acetyllysine; alternate By similarity
Modified residue6051N6-succinyllysine; alternate By similarity
Modified residue6281N6-succinyllysine By similarity
Modified residue6891N6-succinyllysine By similarity
Modified residue7231N6-acetyllysine; alternate By similarity
Modified residue7231N6-succinyllysine; alternate By similarity
Modified residue7301N6-acetyllysine; alternate By similarity
Modified residue7301N6-succinyllysine; alternate By similarity
Modified residue7361N6-acetyllysine By similarity
Modified residue7431N6-acetyllysine By similarity
Cross-link144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict401N → H AA sequence Ref.3
Sequence conflict531N → D AA sequence Ref.3
Sequence conflict991Q → R in CAA90177. Ref.1
Sequence conflict1791E → G in AAI02643. Ref.2
Sequence conflict2171M → T in CAA90177. Ref.1
Sequence conflict4091Q → K AA sequence Ref.3
Sequence conflict4351I → V AA sequence Ref.3
Sequence conflict5551Q → R AA sequence Ref.3
Sequence conflict5771R → K AA sequence Ref.3
Sequence conflict6241V → S AA sequence Ref.3
Sequence conflict6271G → R AA sequence Ref.3
Sequence conflict6521K → Q AA sequence Ref.3
Sequence conflict6741A → S AA sequence Ref.3
Sequence conflict6801H → F AA sequence Ref.3
Sequence conflict7271K → Q AA sequence Ref.3

Secondary structure

................................................................................................................................................... 780
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20004 [UniParc].

Last modified July 11, 2006. Version 4.
Checksum: 91EB21B3923F16C5

FASTA78085,359
        10         20         30         40         50         60 
MAPYSLLVSR LQKALGARQY HVASVLCQRA KVAMSHFEPN EYIRYDLLEK NINIVRKRLN 

        70         80         90        100        110        120 
RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV 

       130        140        150        160        170        180 
PSTIHCDHLI EAQLGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWRPGS GIIHQIILEN 

       190        200        210        220        230        240 
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG 

       250        260        270        280        290        300 
WTSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN 

       310        320        330        340        350        360 
HRMKKYLSKT GRADIANLAD EFKDHLVPDS GCHYDQLIEI NLSELKPHIN GPFTPDLAHP 

       370        380        390        400        410        420 
VAEVGSVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLQC KSQFTITPGS 

       430        440        450        460        470        480 
EQIRATIERD GYAQILRDVG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN 

       490        500        510        520        530        540 
DANPETHAFV TSPEIVTALA IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRAEFDPG 

       550        560        570        580        590        600 
QDTYQHPPKD SSGQQVDVSP TSQRLQLLEP FDKWDGRDLE DLQILIKVKG KCTTDHISAA 

       610        620        630        640        650        660 
GPWLKFRGHL DNISNNLLIG AINVENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI 

       670        680        690        700        710        720 
GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP 

       730        740        750        760        770        780 
VDKLTIKGLK DFAPGKPLTC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQK 

« Hide

References

« Hide 'large scale' references
[1]Xu N., Liu W., Woldegiogis G., Sun X.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Identification of the reactive sulfhydryl and sequences of cysteinyl-tryptic peptides from beef heart aconitase."
Plank D.W., Howard J.B.
J. Biol. Chem. 263:8184-8189(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 28-780.
Tissue: Heart.
[4]"Cysteine labeling studies of beef heart aconitase containing a 4Fe, a cubane 3Fe, or a linear 3Fe cluster."
Plank D.W., Kennedy M.C., Beinert H., Howard J.B.
J. Biol. Chem. 264:20385-20393(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 118-139 AND 439-457, CHARACTERIZATION OF IRON-SULFUR CLUSTERS.
Tissue: Heart.
[5]"Crystal structures of aconitase with isocitrate and nitroisocitrate bound."
Lauble H., Kennedy M.C., Beinert H., Stout C.D.
Biochemistry 31:2735-2748(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-779 IN COMPLEX WITH IRON-SULFUR AND NITROISOCITRATE, REACTION MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49931 mRNA. Translation: CAA90177.1.
BC102642 mRNA. Translation: AAI02643.1.
PIRS57528.
RefSeqNP_776402.1. NM_173977.3.
UniGeneBt.5210.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACOX-ray2.05A29-779[»]
1AMIX-ray2.00A28-779[»]
1AMJX-ray2.00A28-779[»]
1C96X-ray1.81A29-779[»]
1C97X-ray1.98A29-779[»]
1FGHX-ray2.05A29-779[»]
1NISX-ray2.05A29-779[»]
1NITX-ray2.05A29-779[»]
8ACNX-ray2.00A29-779[»]
ProteinModelPortalP20004.
SMRP20004. Positions 29-780.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP20004. 1 interaction.

Proteomic databases

PaxDbP20004.
PRIDEP20004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000008431; ENSBTAP00000008431; ENSBTAG00000006429.
GeneID280976.
KEGGbta:280976.

Organism-specific databases

CTD50.

Phylogenomic databases

eggNOGCOG1048.
GeneTreeENSGT00730000111046.
HOGENOMHOG000224293.
HOVERGENHBG000248.
InParanoidP20004.
KOK01681.
OMAPLKCIIK.
OrthoDBEOG74FF06.
TreeFamTF300627.

Enzyme and pathway databases

UniPathwayUPA00223; UER00718.

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.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF5. PTHR11670:SF5. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsTIGR01340. aconitase_mito. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20004.
NextBio20805079.

Entry information

Entry nameACON_BOVIN
AccessionPrimary (citable) accession number: P20004
Secondary accession number(s): Q3SZZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2006
Last modified: March 19, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways