Aconitate hydratase, mitochondrial precursor

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Q99KI0 (ACON_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aconitate hydratase, mitochondrial
Short name=Aconitase
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase

Gene names

Name:

Aco2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	780 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
PTM	Acetylation Isopeptide bond Phosphoprotein Pyrrolidone carboxylic acid Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	citrate metabolic process Inferred from electronic annotation. Source: Compara isocitrate metabolic process Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrion Inferred from direct assay PubMed 14651853 PubMed 17322295 PubMed 18614015. Source: MGI nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: Compara 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from direct assay PubMed 15317809 PubMed 17322295. Source: MGI citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: Compara isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 27

Mitochondrion By similarity

Chain

28 – 780

753

Aconitate hydratase, mitochondrial

PRO_0000000542

Regions

Region

192 – 194

Substrate binding By similarity

Region

670 – 671

Substrate binding By similarity

Sites

Metal binding

385

Iron-sulfur (4Fe-4S) By similarity

Metal binding

448

Iron-sulfur (4Fe-4S) By similarity

Metal binding

451

Iron-sulfur (4Fe-4S) By similarity

Binding site

Substrate By similarity

Binding site

474

Substrate By similarity

Binding site

479

Substrate By similarity

Binding site

607

Substrate By similarity

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid By similarity

Modified residue

N6-acetyllysine Ref.4

Modified residue

559

Phosphoserine By similarity

Modified residue

573

N6-acetyllysine By similarity

Modified residue

605

N6-acetyllysine By similarity

Cross-link

144

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Experimental info

Sequence conflict

7 – 8

LV → P in BAE25770. Ref.1

Sequence conflict

618

L → F in AAH94462. Ref.2

Sequence conflict

758

F → L in BAE29252. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q99KI0 [UniParc].

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

FASTA

780

85,464

        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' referencesShow '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. 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.
IPI	IPI00116074.
RefSeq	NP_542364.1. NM_080633.2.
UniGene	Mm.154581.
3D structure databases
ProteinModelPortal	Q99KI0.
SMR	Q99KI0. Positions 29-780.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99KI0. 6 interactions.
MINT	MINT-1842680.
PTM databases
PhosphoSite	Q99KI0.
2D gel databases
REPRODUCTION-2DPAGE	Q99KI0.
Proteomic databases
PaxDb	Q99KI0.
PRIDE	Q99KI0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023116; ENSMUSP00000023116; ENSMUSG00000022477.
GeneID	11429.
KEGG	mmu:11429.
UCSC	uc007wxp.1. mouse.
Organism-specific databases
CTD	50.
MGI	MGI:87880. Aco2.
Phylogenomic databases
eggNOG	COG1048.
GeneTree	ENSGT00530000063060.
HOGENOM	HOG000224293.
HOVERGEN	HBG000248.
InParanoid	Q99KI0.
KO	K01681.
OMA	PLKCIIK.
OrthoDB	EOG4BCDM9.
Enzyme and pathway databases
UniPathway	UPA00223; UER00718.
Gene expression databases
Bgee	Q99KI0.
CleanEx	MM_ACO2.
Genevestigator	Q99KI0.
GermOnline	ENSMUSG00000022477. Mus musculus.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
InterPro	IPR015931. 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]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF5. PTHR11670:SF5. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01340. aconitase_mito. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ACO2. mouse.
NextBio	278704.
SOURCE	Search...

Entry information

Entry name

ACON_MOUSE

Accession

Primary (citable) accession number: Q99KI0
Secondary accession number(s): Q3UDK9

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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents