Aconitate hydratase, mitochondrial precursor

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Q9ER34 (ACON_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. History...

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

Documents (2) |

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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.
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	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	citrate metabolic process Inferred from direct assay. Source: RGD isocitrate metabolic process Inferred from direct assay. Source: RGD tricarboxylic acid cycle Inferred from direct assay. Source: RGD
Cellular component	mitochondrion Inferred from direct assay. Source: RGD
Molecular function	3 iron, 4 sulfur cluster binding Inferred from direct assay. Source: RGD 4 iron, 4 sulfur cluster binding Inferred from direct assay. Source: RGD aconitate hydratase activity Inferred from direct assay. Source: RGD citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: RGD
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_0000000544

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 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) By similarity

Experimental info

Sequence conflict

224

L → P in CAC11018. Ref.1

Sequence conflict

295

S → P in CAC11018. Ref.1

Sequence conflict

582

L → Q in CAC11018. Ref.1

Sequence conflict

659

V → M in CAC11018. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ER34 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: E523564299DD38BD
Show »

FASTA

780

85,433

        10         20         30         40         50         60 
MAPYSLLVTR LQKALGVRQY HVASALCQRA KVAMSHFEPS 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 GVKLTGTLSG 

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

       310        320        330        340        350        360 
HRMKKYLSKT GRADIANLAE 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 DFAPGKPLNC IIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the rat heart mitochondrial aconitase." Wieland A., Bruss M. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[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]. Tissue: Prostate.
[3]	Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 32-44; 59-84; 96-138; 143-160; 234-245; 251-302; 313-323; 371-395; 402-409; 412-424; 430-458; 466-474; 480-517; 522-587; 592-628; 634-648; 657-679 AND 694-767, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ243266 mRNA. Translation: CAC11018.1. BC061999 mRNA. Translation: AAH61999.1.
IPI	IPI00421539.
RefSeq	NP_077374.2. NM_024398.2.
UniGene	Rn.43737.
3D structure databases
ProteinModelPortal	Q9ER34.
SMR	Q9ER34. Positions 29-780.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ER34. 1 interaction.
STRING	Q9ER34.
PTM databases
PhosphoSite	Q9ER34.
2D gel databases
World-2DPAGE	0004:Q9ER34.
Proteomic databases
PRIDE	Q9ER34.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000038612; ENSRNOP00000029144; ENSRNOG00000024128.
GeneID	79250.
KEGG	rno:79250.
NMPDR	fig\|10116.3.peg.27460.
UCSC	NM_024398. rat.
Organism-specific databases
CTD	50.
RGD	621360. Aco2.
Phylogenomic databases
eggNOG	roNOG05633.
GeneTree	ENSGT00530000063060.
HOVERGEN	HBG000248.
InParanoid	Q9ER34.
OMA	KHGIRWV.
OrthoDB	EOG4BCDM9.
PhylomeDB	Q9ER34.
Gene expression databases
ArrayExpress	Q9ER34.
Genevestigator	Q9ER34.
GermOnline	ENSRNOG00000024128. Rattus norvegicus.
Family and domain databases
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]
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.
KO	K01681.
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.
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
NextBio	614724.

Entry information

Entry name

ACON_RAT

Accession

Primary (citable) accession number: Q9ER34
Secondary accession number(s): Q6P6V3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	February 1, 2005
Last modified:	November 16, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents