Reviewed, UniProtKB/Swiss-Prot Q99KI0 (ACON_MOUSE)

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)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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.
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 Pyrrolidone carboxylic acid Ubl conjugation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from direct assay. Source: MGI iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion By similarity
	Chain	28 – 780	753	Aconitate hydratase, mitochondrial		PRO_0000000542
Sites
	Metal binding	385	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	448	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	451	1	Iron-sulfur (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	28	1	Pyrrolidone carboxylic acid By similarity
	Modified residue	50	1	N6-acetyllysine Ref.4
	Modified residue	573	1	N6-acetyllysine By similarity
	Modified residue	605	1	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	2	LV → P in BAE25770. Ref.1
	Sequence conflict	618	1	L → F in AAH94462. Ref.2
	Sequence conflict	758	1	F → L in BAE29252. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q99KI0-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9B515846E875D581	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

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. , 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: 16141072] [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: 15489334] [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: 16916647] [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: 17451654] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-144, MASS SPECTROMETRY. Tissue: Heart.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Mm.154581
3D structure databases
HSSP	HSSP built from PDB template 7ACN based on UniProtKB P16276.
SMR	Q99KI0. Positions 29-780.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99KI0. 6 interactions.
STRING	Q99KI0.
PTM databases
PhosphoSite	Q99KI0.
2-D gel databases
REPRODUCTION-2DPAGE	Q99KI0.
Proteomic databases
PRIDE	Q99KI0.
Genome annotation databases
Ensembl	ENSMUST00000023116; ENSMUSP00000023116; ENSMUSG00000022477; Mus musculus. [Genome view]
GeneID	11429.
KEGG	mmu:11429.
NMPDR	fig|10090.3.peg.30319.
UCSC	uc007wxp.1. mouse.
Organism-specific databases
CTD	11429.
MGI	MGI:87880. Aco2.
Phylogenomic databases
HOGENOM	Q99KI0.
HOVERGEN	Q99KI0.
OMA	PGKPLKC.
Enzyme and pathway databases
BRENDA	4.2.1.3. 244.
Gene expression databases
ArrayExpress	Q99KI0.
Bgee	Q99KI0.
CleanEx	MM_ACO2.
Genevestigator	Q99KI0.
GermOnline	ENSMUSG00000022477. Mus musculus.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. 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]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF5. Aconitase_mito. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01340. aconitase_mito. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	278704.
SOURCE	Search...

Entry information

Entry name

ACON_MOUSE

Accession

Primary (citable) accession number: Q99KI0
Secondary accession number(s): Q3UDK9 , Q3ULG9, Q3UNH7, Q505P4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)