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Q99KI0 (ACON_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 97. 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

Catalytic activity

Citrate = isocitrate.

Cofactor

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

Pathway

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

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion By similarity.

Post-translational modification

Acetylation of Lys-50 is observed in liver mitochondria from fasted mice but not from fed mice.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 780753Aconitate hydratase, mitochondrial
PRO_0000000542

Regions

Region192 – 1943Substrate binding By similarity
Region670 – 6712Substrate binding By similarity

Sites

Metal binding3851Iron-sulfur (4Fe-4S) By similarity
Metal binding4481Iron-sulfur (4Fe-4S) By similarity
Metal binding4511Iron-sulfur (4Fe-4S) By similarity
Binding site991Substrate By similarity
Binding site4741Substrate By similarity
Binding site4791Substrate By similarity
Binding site6071Substrate By similarity

Amino acid modifications

Modified residue281Pyrrolidone carboxylic acid By similarity
Modified residue501N6-acetyllysine Ref.4
Modified residue5591Phosphoserine By similarity
Modified residue5731N6-acetyllysine By similarity
Modified residue6051N6-acetyllysine By similarity
Cross-link144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Experimental info

Sequence conflict7 – 82LV → P in BAE25770. Ref.1
Sequence conflict6181L → F in AAH94462. Ref.2
Sequence conflict7581F → L in BAE29252. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q99KI0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9B515846E875D581

FASTA78085,464
        10         20         30         40         50         60 
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPS EYIRYDLLEK NINIVRKRLN 

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

       130        140        150        160        170        180 
PSTIHCDHLI EAQVGGEKDL 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 GRTDIANLAE EFKDHLVPDP GCQYDQVIEI NLNELKPHIN GPFTPDLAHP 

       370        380        390        400        410        420 
VADVGTVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS 

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

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

       550        560        570        580        590        600 
QDTYQHPPKD SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA 

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

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

       730        740        750        760        770        780 
VDKLTIQGLK DFAPGKPLKC VIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow and Kidney.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney and Mammary tumor.
[3]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 32-56; 59-84; 96-138; 143-160; 234-245; 251-258; 313-323; 371-395; 402-409; 412-424; 430-457; 466-474; 480-517; 522-587; 592-605; 608-628; 634-648; 657-671; 694-739 AND 744-767, MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, MASS SPECTROMETRY.
Tissue: Liver.
[5]"A proteomics approach to identify the ubiquitinated proteins in mouse heart."
Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K., Choi H.W., Park Z.-Y., Yoo Y.J.
Biochem. Biophys. Res. Commun. 357:731-736(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-144, MASS SPECTROMETRY.
Tissue: Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK143917 mRNA. Translation: BAE25602.1.
AK144207 mRNA. Translation: BAE25770.1.
AK145511 mRNA. Translation: BAE26479.1.
AK150027 mRNA. Translation: BAE29252.1.
AK165411 mRNA. Translation: BAE38169.1.
BC004645 mRNA. Translation: AAH04645.1.
BC094462 mRNA. Translation: AAH94462.1.
IPIIPI00116074.
RefSeqNP_542364.1. NM_080633.2.
UniGeneMm.154581.

3D structure databases

ProteinModelPortalQ99KI0.
SMRQ99KI0. Positions 29-780.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99KI0. 6 interactions.
MINTMINT-1842680.

PTM databases

PhosphoSiteQ99KI0.

2D gel databases

REPRODUCTION-2DPAGEQ99KI0.

Proteomic databases

PaxDbQ99KI0.
PRIDEQ99KI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023116; ENSMUSP00000023116; ENSMUSG00000022477.
GeneID11429.
KEGGmmu:11429.
UCSCuc007wxp.1. mouse.

Organism-specific databases

CTD50.
MGIMGI:87880. Aco2.

Phylogenomic databases

eggNOGCOG1048.
GeneTreeENSGT00530000063060.
HOGENOMHOG000224293.
HOVERGENHBG000248.
InParanoidQ99KI0.
KOK01681.
OMAPLKCIIK.
OrthoDBEOG4BCDM9.

Enzyme and pathway databases

UniPathwayUPA00223; UER00718.

Gene expression databases

BgeeQ99KI0.
CleanExMM_ACO2.
GenevestigatorQ99KI0.
GermOnlineENSMUSG00000022477. Mus musculus.

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. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01340. aconitase_mito. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACO2. mouse.
NextBio278704.
SOURCESearch...

Entry information

Entry nameACON_MOUSE
AccessionPrimary (citable) accession number: Q99KI0
Secondary accession number(s): Q3UDK9 expand/collapse secondary AC list , Q3ULG9, Q3UNH7, Q505P4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2001
Last modified: May 29, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families